@article{sanders_allen_blankenship_decker_christ-erwin_hentges_jones_mohamedshah_ohlhorst_ruff_et al._2021, title={Implementing the 2020-2025 Dietary Guidelines for Americans: Recommendations for a path forward}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.15969}, abstractNote={AbstractThe Dietary Guidelines for Americans (DGA) provide science‐based recommendations for healthy dietary patterns to promote health and reduce risk of chronic diseases. Yet, since their inception in 1980 and updates every 5 years, Americans fall short of meeting dietary recommendations and diet‐related chronic diseases continue to be a public health concern. In May of 2021, the Institute of Food Technologists and the Department of Food Science at the University of Massachusetts, Amherst, convened a diverse group of thought leaders in health, nutrition, and food science to identify opportunities and approaches to improve consumer adoption of the DGA recommendations. The invited leaders collaborated in roundtable discussions to develop recommendations and strategies to promote adoption of the DGA recommendations after hearing sessions on the latest consumer trends, advances in food science and technology, and effective communications approaches. Participants agreed that changes in consumer behaviors and heightened interest in health due to the novel coronavirus pandemic have created an opportune time to engage consumers about healthy eating. Communications must be simple, tailored to the consumer, and delivered by influencer(s)/spokesperson(s) who are credible sources and share personal values. Innovations in food science and technology have enabled improvements in the safety, health, acceptability, affordability, and availability of foods but opportunities to provide more options to enhance consumption of desired food groups, such as fruits, vegetables, and whole grains, remain. Moving Americans toward healthier dietary patterns aligned with DGA recommendations will require collaborations within the food sector and beyond to achieve broad scale amplification and investment.}, journal={JOURNAL OF FOOD SCIENCE}, author={Sanders, Lisa M. and Allen, Jonathan C. and Blankenship, Jeanne and Decker, Eric A. and Christ-Erwin, Mary and Hentges, Eric J. and Jones, Julie M. and Mohamedshah, Farida Y. and Ohlhorst, Sarah D. and Ruff, John and et al.}, year={2021}, month={Dec} }
 @article{ulus_tekbudak_allen_2021, title={Processing Human Milk to Increase Nutrient Density for Preterm Infants}, ISSN={["1552-5732"]}, DOI={10.1177/08903344211056933}, abstractNote={Background: Human milk is the optimal food for newborns. Choices to feed preterm infants in neonatal intensive care units are mother’s milk, donor milk, or formula. Preterm infants have better tolerance for human milk, but the lower caloric density of donor milk might not meet preterm infant growth needs. Preterm infants have higher protein and energy requirements with a limited stomach capacity. Therefore, there is a need for human milk with increased nutrient density. }, journal={JOURNAL OF HUMAN LACTATION}, author={Ulus, Hande Z. and Tekbudak, Merve Yasemin and Allen, Jonathan C.}, year={2021}, month={Nov} }
 @article{kaufman_jordan_reberg-horton_dean_shew_brandenburg_anco_mehl_taylor_balota_et al._2020, title={Identifying interest, risks, and impressions of organic peanut production: A survey of conventional farmers in the Virginia-Carolina region}, volume={6}, ISSN={["2374-3832"]}, DOI={10.1002/cft2.20042}, abstractNote={Crop, Forage & Turfgrass ManagementVolume 6, Issue 1 e20042 CROP MANAGEMENT—BRIEFS Identifying interest, risks, and impressions of organic peanut production: A survey of conventional farmers in the Virginia–Carolina region Amanda A. Kaufman, Amanda A. Kaufman Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Box 7624, Raleigh, NC, 27695 USASearch for more papers by this authorDavid L. Jordan, Corresponding Author David L. Jordan david_jordan@ncsu.edu orcid.org/0000-0003-4786-2727 Department of Crop and Soil Sciences, North Carolina State University, Box 7620, Raleigh, NC, 27695 USA Correspondence Department of Crop and Soil Sciences, North Carolina State University, Box 7620, Raleigh, NC 27695 Email: david_jordan@ncsu.eduSearch for more papers by this authorChris Reberg-Horton, Chris Reberg-Horton Department of Crop and Soil Sciences, North Carolina State University, Box 7620, Raleigh, NC, 27695 USASearch for more papers by this authorLisa L. Dean, Lisa L. Dean Market Quality and Handling Research Unit, ARS, SEA, USDA, Raleigh, NC, 27695 USASearch for more papers by this authorBarbara B. Shew, Barbara B. Shew Department of Entomology and Plant Pathology, North Carolina State University, Box 7613, Raleigh, NC, 27695 USASearch for more papers by this authorRick L. Brandenburg, Rick L. Brandenburg Department of Entomology and Plant Pathology, North Carolina State University, Box 7613, Raleigh, NC, 27695 USASearch for more papers by this authorDan Anco, Dan Anco Edisto Research and Extension Center, Clemson University, 64 Research Road, Blackville, SC, 29817 USASearch for more papers by this authorHillary Mehl, Hillary Mehl Tidewater Agricultural Research and Extension Center, 6321 Holland Road, Suffolk, VA, 23437 USASearch for more papers by this authorSally Taylor, Sally Taylor Tidewater Agricultural Research and Extension Center, 6321 Holland Road, Suffolk, VA, 23437 USASearch for more papers by this authorMaria Balota, Maria Balota orcid.org/0000-0003-4626-0193 Tidewater Agricultural Research and Extension Center, 6321 Holland Road, Suffolk, VA, 23437 USASearch for more papers by this authorL. Suzanne Goodell, L. Suzanne Goodell Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Box 7624, Raleigh, NC, 27695 USASearch for more papers by this authorJonathan Allen, Jonathan Allen Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Box 7624, Raleigh, NC, 27695 USASearch for more papers by this author Amanda A. Kaufman, Amanda A. Kaufman Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Box 7624, Raleigh, NC, 27695 USASearch for more papers by this authorDavid L. Jordan, Corresponding Author David L. Jordan david_jordan@ncsu.edu orcid.org/0000-0003-4786-2727 Department of Crop and Soil Sciences, North Carolina State University, Box 7620, Raleigh, NC, 27695 USA Correspondence Department of Crop and Soil Sciences, North Carolina State University, Box 7620, Raleigh, NC 27695 Email: david_jordan@ncsu.eduSearch for more papers by this authorChris Reberg-Horton, Chris Reberg-Horton Department of Crop and Soil Sciences, North Carolina State University, Box 7620, Raleigh, NC, 27695 USASearch for more papers by this authorLisa L. Dean, Lisa L. Dean Market Quality and Handling Research Unit, ARS, SEA, USDA, Raleigh, NC, 27695 USASearch for more papers by this authorBarbara B. Shew, Barbara B. Shew Department of Entomology and Plant Pathology, North Carolina State University, Box 7613, Raleigh, NC, 27695 USASearch for more papers by this authorRick L. Brandenburg, Rick L. Brandenburg Department of Entomology and Plant Pathology, North Carolina State University, Box 7613, Raleigh, NC, 27695 USASearch for more papers by this authorDan Anco, Dan Anco Edisto Research and Extension Center, Clemson University, 64 Research Road, Blackville, SC, 29817 USASearch for more papers by this authorHillary Mehl, Hillary Mehl Tidewater Agricultural Research and Extension Center, 6321 Holland Road, Suffolk, VA, 23437 USASearch for more papers by this authorSally Taylor, Sally Taylor Tidewater Agricultural Research and Extension Center, 6321 Holland Road, Suffolk, VA, 23437 USASearch for more papers by this authorMaria Balota, Maria Balota orcid.org/0000-0003-4626-0193 Tidewater Agricultural Research and Extension Center, 6321 Holland Road, Suffolk, VA, 23437 USASearch for more papers by this authorL. Suzanne Goodell, L. Suzanne Goodell Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Box 7624, Raleigh, NC, 27695 USASearch for more papers by this authorJonathan Allen, Jonathan Allen Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Box 7624, Raleigh, NC, 27695 USASearch for more papers by this author First published: 14 June 2020 https://doi.org/10.1002/cft2.20042Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Volume6, Issue12020e20042 RelatedInformation}, number={1}, journal={CROP FORAGE & TURFGRASS MANAGEMENT}, author={Kaufman, Amanda A. and Jordan, David L. and Reberg-Horton, Chris and Dean, Lisa L. and Shew, Barbara B. and Brandenburg, Rick L. and Anco, Dan and Mehl, Hillary and Taylor, Sally and Balota, Maria and et al.}, year={2020} }
 @article{chilungo_muzhingi_truong_allen_2019, title={Effect of processing and oil type on carotene bioaccessibility in traditional foods prepared with flour and puree from orange-fleshed sweetpotatoes}, volume={54}, ISSN={["1365-2621"]}, DOI={10.1111/ijfs.14106}, abstractNote={Summary}, number={6}, journal={INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY}, author={Chilungo, Sarah and Muzhingi, Tawanda and Truong, Van-Den and Allen, Jonathan C.}, year={2019}, month={Jun}, pages={2055–2063} }
 @article{christman_dean_allen_godinez_toomer_2019, title={Peanut skin phenolic extract attenuates hyperglycemic responses in vivo and in vitro}, volume={14}, ISSN={["1932-6203"]}, DOI={10.1371/journal.pone.0214591}, abstractNote={Diabetes affects at least 285 million people globally, and this number continues to increase. Clinical complications include impaired glucose metabolism, hyperglycemia, dyslipidemia, atherosclerosis and non-alcoholic fatty liver disease. Evidence has shown that natural phenolics play a protective effect on both the development and management of type 2 diabetes. This study evaluated effects of the extract from peanut skins containing polyphenols on induced- hyperglycemia using in vivo and in vitro methods. A human hepatocellular liver carcinoma cell line (HepG2) was used to investigate the effect of the peanut skin extract on cell viability after exposure to high glucose concentrations. In vivo, the effect of peanut skin extract on an oral glucose tolerance was investigated in human subjects. Fifteen participants aged 21–32 underwent an oral glucose tolerance test with five treatments: 1) 50-gram glucose solution (reference); 2). 50-gram glucose solution, followed by 12 mg of vegi-capsulated maltodextrin; 3) 50-gram glucose solution, followed by 120 mg of vegi-capsulated maltodextrin-encapsulated peanut skin extract; 4). 50-gram glucose solution, followed by 28 grams of unfortified coated peanuts; 5) 50-gram glucose solution, followed by 28 grams of chili lime coated peanuts fortified with encapsulated peanut skin extract. Glucose levels were measured using a continuous monitor. Peanut skin extract was found to attenuate the decrease in cell viability in high glucose treated HepG2 cells, showing a protective effect against hyperglycemia induced cell death. No difference in the glycemic response area under the curve between any treatments using the tolerance test, but the treatment of the peanut skin extract with the glucose reference resulted in a significantly lower peak blood glucose response at 45 minutes, indicating that it was effective at reducing the glycemic response. The present study shows that the phenolic extract of peanut skins has an antidiabetic effect, further confirming their value as a functional food ingredient.}, number={3}, journal={PLOS ONE}, author={Christman, Lindsey M. and Dean, Lisa L. and Allen, Jonathan C. and Godinez, Sofia Feng and Toomer, Ondulla T.}, year={2019}, month={Mar} }
 @article{ruark_koenning_davis_opperman_lommel_mitchum_sit_2017, title={Incidence and titer of viral infections within soybean cyst nematode culture collections and field populations}, volume={107}, number={1}, journal={Phytopathology}, author={Ruark, C. and Koenning, S. and Davis, E. and Opperman, C. and Lommel, S. and Mitchum, M. G. and Sit, T.}, year={2017}, pages={7–7} }
 @article{meng_perrin_allen_osborne_jones_fogleman_2016, title={Storage of Unfed and Leftover Pasteurized Human Milk}, volume={11}, ISSN={["1556-8342"]}, DOI={10.1089/bfm.2016.0139}, abstractNote={OBJECTIVE
To determine the impact of storage on bacterial growth and immunological activity of pasteurized human milk and leftover pasteurized human milk that has been exposed to the microflora in an infant's mouth.


MATERIALS AND METHODS
Eighteen mother-infant dyads participated in two separate studies. Mother's milk was pasteurized, and each baby was fed 1 to 2 ounces. Pasteurized and leftover pasteurized milk were stored at room (24°C) and refrigerated temperatures (4°C). After storage, milk was analyzed for bacteria, total protein, lysozyme activity, and secretory immunoglobulin A (SIgA) activity.


RESULTS
In pasteurized and leftover pasteurized milk stored in the refrigerator for 7 days, total aerobic bacteria do not increase significantly and total protein and bioactive proteins are stable. At room temperature, there is a significant increase in total aerobic bacteria in leftover pasteurized milk during 12 hours of storage (p < 0.01) and a significant decrease in total protein and SIgA activity in pasteurized milk during 12 hours of storage (p = 0.02 and p = 0.03, respectively).


CONCLUSIONS
When stored in the refrigerator, pasteurized and leftover pasteurized milk may be stored for at least 7 days when considering the variables studied. Caution should be used when storing pasteurized and leftover pasteurized milk at room temperature to prevent an increase in bacterial growth and a decrease in total protein and SIgA activity.}, number={10}, journal={BREASTFEEDING MEDICINE}, author={Meng, Ting and Perrin, Maryanne T. and Allen, Jonathan C. and Osborne, Jason and Jones, Frances and Fogleman, April D.}, year={2016}, month={Dec}, pages={538–543} }
 @article{manavi_alston-mills_thompson_allen_2015, title={Effect of serum cotinine on vitamin D serum concentrations among American females with different ethnic backgrounds}, volume={35}, number={2}, journal={Anticancer Research}, author={Manavi, K. R. and Alston-Mills, B. P. and Thompson, M. P. and Allen, J. C.}, year={2015}, pages={1211–1218} }
 @article{perrin_goodell_allen_fogleman_2014, title={A Mixed-Methods Observational Study of Human Milk Sharing Communities on Facebook}, volume={9}, ISSN={["1556-8342"]}, DOI={10.1089/bfm.2013.0114}, abstractNote={Abstract Objectives: The Food and Drug Administration discourages the casual sharing of human milk because of the risk of pathogen transmission. No information is currently available on the prevalence of this practice. The purpose of this mixed-methods observational study is to describe the size and activity of online milk sharing communities. Materials and Methods: Data for 3 months were extracted from nine public Facebook pages that facilitate the exchange of human milk. The numbers of participants, interactions, and comments were analyzed. Results: We observed 954 individuals participating in milk sharing. The number of interactions per individual ranged from none to 16 (mean, 1.74±1.65). Top reasons that participants requested milk included “lactation problems” (69.4%) and “child health problems” (48.5%). Nearly half of donors were offering 100 ounces or more, which is the minimum to be eligible to donate to nonprofit milk banks. Conclusions: Milk sharing networks in the United States are active, with...}, number={3}, journal={BREASTFEEDING MEDICINE}, author={Perrin, Maryanne Tigchelaar and Goodell, L. Suzanne and Allen, Jonathan C. and Fogleman, April}, year={2014}, month={Apr}, pages={128–134} }
 @article{maloney_truong_allen_2014, title={Susceptibility of sweet potato (Ipomoea batatas) peel proteins to digestive enzymes}, volume={2}, ISSN={2048-7177}, url={http://dx.doi.org/10.1002/FSN3.110}, DOI={10.1002/FSN3.110}, abstractNote={Abstract}, number={4}, journal={Food Science & Nutrition}, publisher={Wiley}, author={Maloney, Katherine P. and Truong, Van-Den and Allen, Jonathan C.}, year={2014}, month={Apr}, pages={351–360} }
 @article{perrin_fogleman_allen_2013, title={The Nutritive and Immunoprotective Quality of Human Milk beyond 1 Year Postpartum: Are Lactation-Duration-Based Donor Exclusions Justified?}, volume={29}, ISSN={["1552-5732"]}, DOI={10.1177/0890334413487432}, abstractNote={ Donor human milk is critical for the fragile preterm infant who does not have access to his or her mother’s milk, improving survival rates and quality of survival and decreasing hospital stay. Despite the opening of donor milk banks around the world, shortages continue as demand for donor milk exceeds supply. One potential means of increasing supply is by reducing exclusion criteria that prohibit mothers from donating milk based on duration of lactation. Minimal research has been done on the composition of human milk during the second year of lactation, with most research focusing on the nutritive compounds and not the immunoprotective compounds. Several immunoprotective compounds, including lysozyme, lactoferrin, secretory immunoglobulin A, and oligosaccharides, are abundant in human milk compared to bovine-based infant formula and are partially or fully retained during Holder pasteurization, making them an important differentiating feature of donor milk. A PubMed search was conducted to review studies in human milk composition during the second year of lactation. Limitations of existing research include sample collection protocols, small study sizes, and use of populations that may have been at risk for nutritional deficiencies. Stable concentrations of several components were reported including protein, lactose, iron, copper, lactoferrin, and secretory immunoglobulin A. Lysozyme concentration increased during extended lactation, while zinc and calcium concentrations declined into the second year. Conflicting findings were reported on fat content, and no information was available regarding oligosaccharide content. More research is needed to create evidence-based guidelines regarding the nutritive and immunoprotective value of donor milk throughout the course of lactation. }, number={3}, journal={JOURNAL OF HUMAN LACTATION}, author={Perrin, Maryanne Tigchelaar and Fogleman, April and Allen, Jonathan C.}, year={2013}, month={Aug}, pages={341–349} }
 @article{maloney_truong_allen_2012, title={Chemical Optimization of Protein Extraction from Sweet Potato (Ipomoea batatas) Peel}, volume={77}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2012.02921.x}, abstractNote={Abstract:  Proteins isolated from sweet potatoes (Ipomoea batatas) have been shown to possess antidiabetic, antioxidant, and antiproliferative properties. The objective of this study was to chemically optimize a process for extracting proteins from sweet potato peel. The extraction procedure involved mixing peel with saline solvent to dissolve proteins and then precipitating with CaCl2. Quadratic and segmented models were used to determine the optimum NaCl concentration and peel to solvent ratio to maximize protein solubility while minimizing solvent usage. A segmented model was also used to optimize the concentration of CaCl2 used for precipitation. The highest yield was obtained by mixing blanched peelings with 59.7 mL of 0.025 mM NaCl per g peel and then precipitating with 6.8 mM CaCl2. The results of this study show that potentially valuable proteins can be extracted from peel generated during processing of sweet potatoes and industrial costs can be minimized by using these optimum conditions.}, number={11}, journal={JOURNAL OF FOOD SCIENCE}, author={Maloney, Katherine P. and Truong, Van-Den and Allen, Jonathan C.}, year={2012}, month={Nov}, pages={E307–E312} }
 @misc{asghar_anjum_allen_2011, title={Utilization of Dairy Byproduct Proteins, Surfactants, and Enzymes in Frozen Dough}, volume={51}, ISSN={["1549-7852"]}, DOI={10.1080/10408391003605482}, abstractNote={Use of natural additives is gaining popularity among the masses as they are becoming more conscious about their diet and health. Frozen dough products are one of the recent examples of value-added cereal products which face stability problems during extended storage periods of times. Dairy whey proteins, surfactants, and certain enzymes are considered important natural additives which could be used to control the water redistribution problem in the dough structure during the storage condition. They interact with the starch and gluten network in a dough system and thus behave as dough improvers and strengtheners. These natural additives not only help to bind extra moisture but also to improve texture and sensory attributes in frozen dough bakery products.}, number={4}, journal={CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION}, author={Asghar, Ali and Anjum, Faqir Muhammad and Allen, Jonathan C.}, year={2011}, pages={374–382} }
 @article{asghar_anjum_allen_daubert_rasool_2009, title={Effect of modified whey protein concentrates on empirical and fundamental dynamic mechanical properties of frozen dough}, volume={23}, ISSN={["0268-005X"]}, DOI={10.1016/j.foodhyd.2009.01.005}, abstractNote={Dairy byproduct proteins are considered natural functional additives having the ability to interact with the starch and gluten network in a dough system and thus behave as dough improvers. Native whey proteins have negative effect in bread making so whey protein concentrates modified to increase viscosity in solution (mWPC) might overcome undesirable weakening of the gluten network which usually occurs in frozen dough products during prolonged times in frozen storage. The objective of this research project was to determine the effect of mWPC on empirical and fundamental dynamic rheological properties of wheat flour dough. The results for empirical rheological studies showed that addition of mWPC had significant effects on mixographic parameters and also increased values of mixing time and peak height percentage. The results for the fundamental mechanical properties of the frozen dough revealed an increase in the values of G′ with the increase in the frequency, along with an upward trend with increasing temperature, but the highest values were obtained after cooling. Addition of mWPC in the dough treatments induced softening in the dough system, as shown by the decrease in the values of the viscoelastic moduli. Rheological and textural changes in the bakery products made from frozen dough could be imparted by the incorporation of modified whey protein concentrates as dough improvers.}, number={7}, journal={FOOD HYDROCOLLOIDS}, author={Asghar, Ali and Anjum, Faqir Muhammad and Allen, Jonathan C. and Daubert, Christopher R. and Rasool, Ghulam}, year={2009}, month={Oct}, pages={1687–1692} }
 @article{mcclelland_allen_zakir_2007, title={Bio-Medicinal Effect of Sweet Potato in People with Diabetes}, volume={107}, ISSN={0002-8223}, url={http://dx.doi.org/10.1016/j.jada.2007.05.396}, DOI={10.1016/j.jada.2007.05.396}, abstractNote={Discuss the potential application of sweet potatoes in the diet of persons with diabetes}, number={8}, journal={Journal of the American Dietetic Association}, publisher={Elsevier BV}, author={McClelland, J.W. and Allen, J.C. and Zakir, S.}, year={2007}, month={Aug}, pages={A104} }
 @article{viazis_farkas_allen_2007, title={Effects of high-pressure processing on immunoglobulin A and lysozyme activity in human milk}, volume={23}, ISSN={["1552-5732"]}, DOI={10.1177/0890334407303945}, abstractNote={Banked human milk, processed using low-temperature/long-time or Holder pasteurization, inactivates pathogenic microorganisms but degrades important biochemical components. High-pressure processing kinetics favor inactivation of microorganisms with retention of biochemical activity and nutritional quality of foods. The effects of high-pressure processing (400 MPa) and low-temperature/long-time pasteurization (62.5°C, 30 minutes) on total immunoglobulin A and lysozyme activity in human milk were investigated. Indirect modified enzyme-linked immunosorbent and a Micrococcus lysodeikticus turbidimetric assay were performed to measure immunoglobulin A immunoactivity and lysozyme activity, respectively. Pressure-treated samples retained significantly higher ( P < .05) levels of immunoglobulin A and lysozyme activity compared to samples treated with low-temperature/ long-time pasteurization. These data suggest that high-pressure processing is a potential alternative to thermal pasteurization of human milk that can give greater retention of some bioactive components. Further research is needed to determine whether high-pressure processing can inactivate pathogens of concern in donor human milk. J Hum Lact. 23(3):253-261.}, number={3}, journal={JOURNAL OF HUMAN LACTATION}, author={Viazis, Stelios and Farkas, Brian E. and Allen, Jonathan C.}, year={2007}, month={Aug}, pages={253–261} }
 @article{sauls_arnold_bell_allen_hoffman_2007, title={Pro-thrombotic and pro-oxidant effects of diet-induced hyperhomocysteinemia}, volume={120}, ISSN={0049-3848}, url={http://dx.doi.org/10.1016/j.thromres.2006.08.001}, DOI={10.1016/j.thromres.2006.08.001}, abstractNote={Elevated plasma homocysteine levels are associated with the risk of atherosclerosis and arterial and venous thrombosis. We have previously demonstrated that rabbits rendered hyperhomocysteinemic by parenteral administration of homocysteine develop a dysfibrinogenemia that is associated with the formation of fibrin clots that are abnormally resistant to fibrinolysis. We suggested that this acquired dysfibrinogenemia contributes to the thrombotic tendency in hyperhomocysteinemia. However, it was possible that the homocysteine-associated dysfibrinogenemia was an artifact of the parenteral administration model. Therefore, the goals of the current study were to develop a diet-induced model of homocysteinemia in rabbits and determine whether a dysfibrinogenemia and evidence of oxidative stress develop in this model as they do when homocysteine is injected. We found that rabbits fed a diet severely deficient in folate and mildly deficient in choline develop mild hyperhomocysteinemia: 14.8±4.0 μM in deficient rabbits compared to 9.0±1.7 μM in controls. The deficient rabbits also develop evidence of oxidant stress: increased lipid peroxidation in liver, impaired mitochondrial enzyme activities in liver and elevated caspase-3 levels in plasma. Most importantly, the deficient rabbits also develop a dysfibrinogenemia characterized by increased resistance to fibrinolysis. We believe that this dietary model of homocysteinemia is clinically relevant and reproduces many features associated with hyperhomocysteinemia in previous work using in vitro and in vivo models. Our findings suggest that an acquired dysfibrinogenemia could play a role in the increased risk of atherothrombotic disease in mildly hyperhomocysteinemic human subjects.}, number={1}, journal={Thrombosis Research}, publisher={Elsevier BV}, author={Sauls, Derrick L. and Arnold, Erin K. and Bell, Charles W. and Allen, Jonathan C. and Hoffman, Maureane}, year={2007}, month={Jan}, pages={117–126} }
 @article{allen_allen_boyd_alston-mills_fenner_2006, title={Determination of membrane lipid differences in insulin resistant diabetes mellitus type 2 in whites and blacks}, volume={22}, ISSN={["0899-9007"]}, DOI={10.1016/j.nut.2006.07.007}, abstractNote={Insulin resistance in diabetes mellitus type 2 (DM2) can result from membrane lipid alterations. Blacks are at a higher risk of developing DM2; therefore, we investigated whether membrane lipid differences exist between blacks and whites and if differences contribute to impaired insulin binding in diabetes. Subjects were recruited from four groups: white control (n = 10), black control (n = 10), white diabetic (n = 5), and black diabetic (n = 10). Diabetic subjects who had DM2 with insulin resistance on insulin monotherapy were matched by age and sex. The following determinations were made: fasting serum glucose, fasting serum insulin, plasma lipid profile, red blood cell (RBC) membrane lipids and cholesterol, and RBC insulin binding. The membrane lipid analysis showed racial differences in phosphatidyl ethanolamine (PE) and phosphatidyl choline (PC). The plasma membrane of whites showed higher PE and lower PC levels than that in blacks. The RBC rheologic (PE/phosphatidyl serine) properties (deformability) were lower in diabetics and black subjects. The saturated nature of RBC ([sphingomyelin + PC)/(PE + phosphatidyl serine]) was the lowest in white control subjects (P < 0.056). The combination of increased saturated/polyunsaturated fatty acids, increased saturated nature, and increased cholesterol/phospholipid can contribute to decreased membrane fluidity, resulting in insulin resistance. Also, decreased RBC deformability can make oxygen delivery through the capillaries difficult, create tissue hypoxia, and contribute to some of the known complications of diabetes. Membrane lipid alteration may be one of the reasons for a higher incidence of diabetes among blacks.}, number={11-12}, journal={NUTRITION}, author={Allen, Hengameh G. and Allen, Jonathan C. and Boyd, Leon C. and Alston-Mills, Brenda P. and Fenner, Gregory P.}, year={2006}, pages={1096–1102} }
 @article{banini_boyd_allen_allen_sauls_2006, title={Muscadine grape products intake, diet and blood constituents of nondiabetic and type 2 diabetic subjects}, volume={22}, ISSN={["1873-1244"]}, DOI={10.1016/j.nut.2006.08.012}, abstractNote={Red wines and grape juices contain polyphenolics with antioxidant and antiplatelet properties that may be protective against oxidative stress leading to hypertension, insulin resistance, and type 2 diabetes (T2D). This study evaluated the effects of supplementing meals of subjects with 150 mL of muscadine grape juice (MJ), muscadine grape wine (MW), and dealcoholized muscadine grape wine (Dz-W) on glycemic indices, blood constituents, lipid profile, anthropometric, and nutrient intakes of healthy and T2D subjects over a 28-d period. Subjects with T2D were assigned to take MJ, MW, or Dz-W. Non-diabetics consumed MJ and controls were given no test drinks. Several metabolic indicators associated with diabetic conditions were measured at baseline and repeated after 28 d. Diabetics given MW and Dz-W showed lower levels of blood glucose, insulin, and glycated hemoglobin, indicating better glycemic control. Elevated dietary vitamin C and E levels were observed in diabetics given Dz-W, indicating improved antioxidant status. Decreased red blood cell membrane saturated fatty acids and increased mono- and polyunsaturated fatty acids for subjects with T2D given MW suggested improved membrane fluidity. Lower sodium and chloride values for subjects T2D given MW suggested lower risk for developing hypertension. Improved hepatic conditions were noted by decreases in alanine aminotransferase and aspartate aminotransferase among subjects with T2D given MW, indicating better insulin sensitivity and decreased tendency toward impaired liver function. Daily intake of 150 mL of MW or Dz-W with meals improved several metabolic responses among diabetics compared with diabetics given MJ.}, number={11-12}, journal={NUTRITION}, author={Banini, Akpene E. and Boyd, Leon C. and Allen, Jonathan C. and Allen, Hengameh G. and Sauls, Derrick L.}, year={2006}, pages={1137–1145} }
 @article{sauls_boyd_allen_hoffman_2004, title={Differences in the metabolic response to exogenous homocysteine in juvenile and adult rabbits}, volume={15}, DOI={10.1016/j.nutbio.2003.09.010}, number={2}, journal={Journal of Nutritional Biochemistry}, author={Sauls, D. L. and Boyd, L. C. and Allen, J. C. and Hoffman, M.}, year={2004}, pages={96–102} }
 @article{sauls_boyd_allen_hoffman_2004, title={Differences in the metabolic response to exogenous homocysteine in juvenile and adult rabbits}, volume={15}, ISSN={0955-2863}, url={http://dx.doi.org/10.1016/j.jnutbio.2003.09.010}, DOI={10.1016/j.jnutbio.2003.09.010}, abstractNote={Homocysteine has recently received a lot of attention as an independent risk factor for atherosclerotic and thrombotic cardiovascular disease. Plasma homocysteine levels tend to rise with age, but are also greatly influenced by nutritional factors. Early reports suggested that there were differences in the metabolism of homocysteine in adult and immature animals. The current work tests the hypothesis that adult and juvenile animals respond differently to chronic administration of homocysteine. We have previously found that adult rabbits given homocysteine parenterally twice daily for seven weeks developed progressive folate deficiency and concurrently developed an impairment of homocysteine metabolism. We now report that juvenile rabbits do not develop folate deficiency with chronic homocysteine loading and do not have progressively higher trough levels of homocysteine, as do the adults. In addition, juvenile rabbits that have been chronically pre-treated with homocysteine exhibit a lower peak homocysteine level after a single dose than do juvenile rabbits that have never received homocysteine. This adaptation did not occur in the adult rabbits. In addition, adult homocysteine-treated rabbits had evidence of oxidative stress as evidenced by higher levels of malondialdehyde in liver tissue than adult controls. The homocysteine-treated juvenile rabbits had the same levels of malondialdehyde as the juvenile control rabbits. We conclude that the plasma elimination kinetics are altered in juvenile rabbits in response to homocysteine pre-treatment. The difference in metabolism of homocysteine may protect the juvenile rabbits from the damaging effects of homocysteine. Future studies are planned to elucidate the mechanism of this adaptive response.}, number={2}, journal={The Journal of Nutritional Biochemistry}, publisher={Elsevier BV}, author={Sauls, Derrick L. and Boyd, Leon C. and Allen, Jonathan C. and Hoffman, Maureane}, year={2004}, month={Feb}, pages={96–102} }
 @article{allen_allen_boyd_alston-mills_2003, title={Can anthropometric measurements and diet analysis serve as useful tools to determine risk factors for insulin-resistant diabetes type 2 among white and black Americans?}, volume={19}, ISSN={["0899-9007"]}, DOI={10.1016/S0899-9007(03)00090-X}, abstractNote={Central obesity is implicated in the development of insulin resistance by increasing insulin demand and eventually leading to hyperinsulinemia. Anthropometric measurements have been helpful in determining the risk factors in developing diabetes mellitus type 2. In this study we investigated whether anthropometric measurements differ among diabetics of different races. We also evaluated whether nutrient intake of these individuals was related to anthropometric measurement changes.Subjects were recruited from four groups: white control (n = 10), black control (n = 10), white diabetic (n = 5), and black diabetic (n = 10). The diabetic subjects had type 2 diabetes with insulin resistance on insulin monotherapy (age and sex matched). The following determinations were made: diet analysis, body mass index (kg/m(2)), the ratio of waist (umbilical level) to hip (maximum at buttocks) circumference, the ratio of waist to thigh (mid-thigh), and body fat percentage.The micronutrient consumption was fairly similar in all groups with the exception of vitamin A (greatest consumption in the white control group, P < 0.05; and the lowest consumption in the black control group, P < 0.05). The data also suggested that central obesity (greatest waist-to-hip ratio) was present in the individuals with type 2 diabetes. The higher total fat, including saturated, monounsaturated, polyunsaturated, and cholesterol, intake in the diabetic groups were observed.The type of fat consumed may be as important as the total fat consumption in the development of insulin resistance. The diet analysis can provide valuable information about the dietary habits of an individual and the possible causes of metabolic problems leading to a disease state. However, genetic factors must be considered when looking at diabetes incidence in different ethnic groups. For example, even though the black diabetic group consumed less fat in comparison with the other groups, their body fat percentages were higher. Therefore, we cannot conclude that high fat intake is primarily responsible for increased body fat percentage. Although anthropometric measurements are a useful tool in risk assessment, researchers should consider anatomic differences among different racial groups as covariables. Diet analysis when used in conjunction with anthropometric measurements can serve as a useful tool to detect whether metabolic alterations are related to dietary habits.}, number={7-8}, journal={NUTRITION}, author={Allen, HG and Allen, JC and Boyd, LC and Alston-Mills, BP}, year={2003}, pages={584–588} }
 @article{banini_allen_allen_boyd_lartey_2003, title={Fatty acids, diet, and body indices of type II diabetic American whites and blacks and Ghanaians}, volume={19}, ISSN={["0899-9007"]}, DOI={10.1016/S0899-9007(03)00108-4}, abstractNote={This research was designed to study the diet, lipid profile, and metabolic and body indices of type II diabetic and non-diabetic subjects among American white and black and Ghanaian populations.Fifty-one type II diabetic and non-diabetic volunteers were recruited through medical clinics. Data collected included food intake and anthropometric measurement. Blood samples were taken for glucose and serum lipid analyses. Serum non-esterified fatty acids, very low-density lipoproteins, low-density lipoproteins, high-density lipoproteins, total cholesterol, and triacylglycerols levels were measured.The Ghanaian subjects had lower body mass indexes than did the American white and black subjects (P < 0.01), although they recorded the highest carbohydrate intake. Dietary fat intake was not significantly correlated with body fat level or body mass index among the different observational groups. The serum ratio of saturated to polyunsaturated fat was higher in all diabetics than in controls and higher in Ghanaians than in Americans. Total cholesterol, triacylglycerols, and lipoproteins were within normal ranges for diabetic and non-diabetic subjects. The ratio of total cholesterol to high-density lipoprotein cholesterol was slightly elevated among the white diabetics (P < 0.05).The data showed a higher metabolism of carbohydrate for energy in the Ghanaian group than in the other groups. In addition, fat metabolism may differ between Americans and Ghanaians. For many variables, black Americans were more similar to white Americans than to Ghanaians. These observations imply that cultural factors may contribute more than ethnic origin to the etiology of diabetes.}, number={9}, journal={NUTRITION}, author={Banini, AE and Allen, JC and Allen, HG and Boyd, LC and Lartey, A}, year={2003}, month={Sep}, pages={722–726} }
 @article{sternhagen_allen_2001, title={Growth rates of a human colon adenocarcinoma cell line are regulated by the milk protein alpha-lactalbumin}, DOI={10.1007/978-1-4615-1371-1_14}, abstractNote={The whey protein alpha-lactalbumin, derived from human milk, has been shown to inhibit proliferation of mammary epithelial cells and rat kidney cells. We have shown that bovine alpha-lactalbumin also has antiproliferative effects in human colon adenocarcinoma cell lines. During a 5-day dose-dependent growth study, bovine alpha-lactalbumin was added to Caco-2 or HT-29 monolayers in amounts from 5 to 35 microg/mL. Low concentrations of alpha-lactalbumin (10-25 microg/mL) stimulated growth during the first 3 to 4 days. After growing for 4 days, proliferation ceased and viable cell numbers decreased dramatically in the alpha-lactalbumin-treated cultures, suggesting a delayed initiation of apoptosis. This experiment demonstrates the acute bioactive effects of small concentrations of alpha-lactalbumin, compared with the high concentrations of other proteins in the media. These results suggest that alpha-lactalbumin in milk may promote health by inhibiting growth of potential cancer cells. Further studies will identify the role of calcium in the bioactivity of alpha-lactalbumin.}, journal={Bioactive components of human milk (Advances in experimental medicine and biology; v. 501)}, publisher={New York: Kluwer Academic/Plenum Publishers}, author={Sternhagen, L. G. and Allen, J. C.}, year={2001}, pages={115–120} }
 @article{chen_allen_2001, title={Human milk antibacterial factors - The effect of temperature on defense systems}, DOI={10.1007/978-1-4615-1371-1_42}, abstractNote={Bovine milk will eventually spoil at refrigeration temperatures, but endogenous or exogenous pathogenic or spoilage bacteria in human milk stored for delayed feeding will die. We investigated the mechanism for these antibacterial properties and their response to high-tempertature, short-time (HTST, 72°C-75°C, 15 sec) and low-temperature long-time (LTLT, 65°C, 30min) pasteurization. NonpathogenicListeria innocua(106cfu/mL) was inoculated into raw and processed bovine and human milk; bacterial plate counts twice weekly determined antibacterial activities. Up to 99% ofL. innocuawere killed and further growth was inhibited in raw and pasteurized human milk for at least 60 days at 4°C. Reactive IgA antibodies againstListeriaantigens were demonstrated by enzyme immunoassay in some human milk samples; sIgA activity againstEscherichia coliO antigens was significantly decreased by heat treatments (raw, 1.8; HTST, 1.1; LTLT, 1.3 activity units). Adding human lactoferrin (0.5-20 mg/mL) to theListeriainoculum (-107cfu/mL) in 1% peptone water did not inhibit bacterial growth.}, journal={Bioactive components of human milk (Advances in experimental medicine and biology; v. 501)}, publisher={New York: Kluwer Academic/Plenum Publishers}, author={Chen, H. Y. and Allen, J. C.}, year={2001}, pages={341–348} }
 @misc{swaisgood_wang_allen_2001, title={Protein ingredient for carrying lipophilic nutrients}, volume={6,290,974}, number={2001 Sept. 18}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Swaisgood, H. E. and Wang, Q.-W. and Allen, J. C.}, year={2001} }
 @article{park_allen_2000, title={Antigenicity of casein phosphopeptides prepared with immobilized glutamic acid-specific endopeptidase or trypsin}, volume={20}, ISSN={["0271-5317"]}, DOI={10.1016/s0271-5317(00)00129-9}, abstractNote={The antigencity of phosphopeptides derived from the hydrolysis of αs- or β-casein with trypsin or glutamic acid-specific endopeptidase (GSE) was studied using a rat model system. Relative levels of specific IgG and IgE made in response to intraperitoneal sensitization to tryptic or GSE hydrolysates of αs- or β-casein or derivatives were determined using indirect and amplified indirect ELISA, respectively. Serum was tested for antibodies to whole, αs- or β-casein. More reactive IgG against whole and αs-casein than β-casein was expressed. Hydrolysis of αs- or β-casein with either trypsin or GSE did not reduce antigenicity relative to intact protein, but tryptic αs-casein phosphopeptides were significantly less antigenic than intact αs-casein and its hydrolysates. The antigenicity of tryptic hydrolysis was less than that of GSE hydrolysis. These results suggest that tryptic phosphopeptides could be used as a food ingredient with hypoallergenicity.}, number={3}, journal={NUTRITION RESEARCH}, author={Park, OJ and Allen, JC}, year={2000}, month={Mar}, pages={359–370} }
 @article{wang_allen_swaisgood_1999, title={Binding of lipophilic nutrients to beta-lactoglobulin prepared by bioselective adsorption}, volume={82}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(99)75231-8}, abstractNote={The binding of the lipophilic nutrients, retinal, vitamin D2, and retinyl palmitate by beta-lactoglobulin was measured by analysis of changes in the fluorescence of the tryptophanyl residue of beta-lactoglobulin or the retinyl moiety. The fluorescence intensity of the tryptophanyl residue was quenched by retinoid or vitamin D binding but was enhanced by palmitate binding. The analysis of competitive binding experiments with palmitate indicated that retinal and palmitate did not compete for the same site; however, vitamin D2, which binds with a stoichiometry of 2, appeared to displace palmitate at higher concentrations. Also, the retinoids and vitamin D2 were bound more tightly than was palmitate. The results are consistent with the model in which the retinoids and vitamin D2 bind in the calyx formed by the beta-barrel; palmitate and a second molecule of vitamin D2 bind in a surface pocket near the dimer contact region. Retinyl palmitate, which has both moieties, appeared to bind at both sites.}, number={2}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QW and Allen, JC and Swaisgood, HE}, year={1999}, month={Feb}, pages={257–264} }
 @misc{alston-mills_hepler_sternhagen_allen_meshaw_1998, title={Alpha-lactalbumin as a modulator of mammary cellular activity}, volume={34}, DOI={10.1007/s11626-998-0026-9}, number={10}, journal={In Vitro Cellular & Developmental Biology. Animal}, author={Alston-Mills, B. and Hepler, C. D. and Sternhagen, L. and Allen, J. C. and Meshaw, K. A.}, year={1998}, pages={747–750} }
 @article{park_swaisgood_allen_1998, title={Calcium binding of phosphopeptides derived from hydrolysis of alpha(s)-Casein or beta-Casein using immobilized trypsin}, volume={81}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(98)75844-8}, abstractNote={Abstract Calcium binding to casein phosphopeptides that were derived from α s -CN or β -CN was studied. Purified α s -CN or β -CN was prepared from fresh skim milk using an anion-exchange column. Peptides were prepared by casein hydrolysis using a fluidized bed bioreactor containing 2ml of immobilized trypsin (activity: 49.4 U/g of beads). The disappearance of intact protein and the appearance of products of low molecular mass were monitored by SDS-PAGE. α s -Casein and β -CN hydrolysates were loaded on an anion-exchange column, followed by stepwise elution with 0, 0.1, 0.2, 0.4, and 0.5 M KCl in equilibration buffer to separate the phosphopeptides from the other casein peptides. Protein and P were measured in the elution peaks. Calcium binding to each fraction was determined with a Ca-selective electrode. Electrophoresis showed that intact proteins were hydrolyzed rapidly, and peptides appeared on the gel in greater concentrations as the incubation time increased. The major products were a main band with a molecular mass of 6.2 kDa from β -CN hydrolysates and a series of bands from 4.0 to 12.8 kDa from a α s -CN hydrolysate. The greatest yield and concentration of phosphate from β -CN hydrolysate were found in the peak that eluted with 0.4 M KCl in equilibration buffer and for α s -CN in the peak that eluted with 0.1 M KCl. The α s -CN phosphopeptides showed greater Ca 2+ binding than the phosphopeptides from β -CN. Separation of casein phosphopeptides using anion exchange was not specific. However, results showed that each peak containing high concentrations of phosphate had Ca 2+ -binding ability. Further characterization of these casein phosphopeptides might result in a Ca-complexing food ingredient.}, number={11}, journal={JOURNAL OF DAIRY SCIENCE}, author={Park, O and Swaisgood, HE and Allen, JC}, year={1998}, month={Nov}, pages={2850–2857} }
 @article{park_allen_1998, title={Preparation of phosphopeptides derived from alpha(s)-casein and beta-casein using immobilized glutamic acid-specific endopeptidase and characterization of their calcium binding}, volume={81}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(98)75845-X}, abstractNote={Abstract Phosphopeptides that were derived from α s -CN or β -CN were prepared with immobilized glutamic acid-specific endopeptidase, and their Ca 2+ binding was characterized. α s -Casein or β -CN was hydrolyzed in a fluidized bed bioreactor containing 2ml of immobilized glutamic acid-specific endopeptidase by recirculating 20ml of α s -CN or β -CN solution (10 mg/ml in 50mM Tris·HCl and 0.02% NaN 3 , pH 8.0) for 3h at 20°C. The molecular masses of casein peptides were monitored by SDS-PAGE. Each hydrolysate was applied to an anion-exchange column using stepwise elution with various concentrations of KCl to separate peptides. The casein phosphopeptide content of the elution profile was monitored by analysis of protein and P concentrations. Calcium binding in phosphopeptide-enriched fractions was determined by CaCl 2 titration and measurement of free Ca 2+ with a Ca-selective electrode. The electrophoresis patterns showed four major peptides having molecular masses of 10.8, 9.0, 6.6, and 3.6 kDa in the α s -CN hydrolysate and 9.3, 8.2, and 6.2 kDa in the β -CN hydrolysate. The highest concentrations of P were detected in the fractions that eluted with 0.4 and 0.5M KCl for the α s -CN hydrolysate and with 0.4 M KCl for the β -CN hydrolysate. The calcium-binding ability was found only in the fraction that was eluted with 0.4 M KCl; the maximum Ca 2+ binding and the apparent binding constant were 0.24 mmol/mg of protein and 75 M –1 , and 0.14 mmol/mg of protein and 148 M –1 , respectively. α s -Casein phosphopeptides had different patterns for Ca 2+ binding than did β -CN phosphopeptides as the total Ca concentration was increased. Calcium binding to these casein phosphopeptides differed from that previously characterized for the tryptic peptides.}, number={11}, journal={JOURNAL OF DAIRY SCIENCE}, author={Park, O and Allen, JC}, year={1998}, month={Nov}, pages={2858–2865} }
 @article{wang_allen_swaisgood_1998, title={Protein concentration dependence of palmitate binding to beta-lactoglobulin}, volume={81}, ISSN={["1525-3198"]}, DOI={10.3168/jds.S0022-0302(98)75553-5}, abstractNote={Abstract The binding of palmitate to β -lactoglobulin at protein concentrations ranging from 1 to 200 μM was determined using an ultrafiltration method with [ 14 C]palmitate. Fit of the data to theoretical models required the assumption of two independent sets of binding sites; however, binding characteristics were dependent on the protein concentration. A model assuming one set of sites on the protein monomer and another on the dimer was consistent with the data. The analysis suggests that 2mol of palmitate are bound/mol of dimer and that the binding constant is of the order of 10 5 M –1 ; a larger number of palmitate molecules are bound per mole of monomer with a smaller binding constant of the order of 10 4 M –1 . Apparently, formation of the dimer, by hydrophobic interactions at the monomer contact site, eliminated palmitate binding sites on the monomer but formed a higher affinity pocket for binding to the dimer.}, number={1}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QWQ and Allen, JC and Swaisgood, HE}, year={1998}, month={Jan}, pages={76–81} }
 @article{wang_allen_swaisgood_1997, title={Binding of retinoids to beta-lactoglobulin isolated by bioselective adsorption}, volume={80}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(97)76029-6}, abstractNote={Abstract Binding of the retinoids, all-trans -retinol, all- trans -retinal, all-trans -retinyl acetate, and all-trans -retinoic acid, to β-lactoglobulin (LG) (96% purity) that had been prepared by bioselective adsorption on N-retinyl-Celite TM was determined from changes in the fluorescence quenching (332nm) of the protein tryptophanyl residues. High affinity binding of all of these compounds occurred at pH 7.0, and the apparent dissociation constant ranged from 1.7 to 3.6 × 10 –8 M . Furthermore, a stoichiometry of 1.0 mol·mol –1 of protein was obtained for each case, indicating that all of the sites in the protein preparation were available. When β-LG in whey protein isolate (57.4% β-LG) was studied, a stoichiometry of 0.65 to 0.82 mol·mol –1 of protein was obtained, indicating that a large number of the sites already had bound lipid or that the protein had been denatured. As the pH was lowered toward 5.15, the affinity decreased about fourfold, but the stoichiometry of binding was unchanged. Far UV circular dichroism spectra indicated that the secondary structure of the protein was not significantly affected by ligand binding; however, the near UV spectra were changed, indicating that the flexibility of tryptophanyl residues decreased. The latter effect is consistent with the change in fluorescence quenching and suggests that a tryptophan is in the binding site.}, number={6}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QW and Allen, JC and Swaisgood, HE}, year={1997}, month={Jun}, pages={1047–1053} }
 @article{wang_allen_swaisgood_1997, title={Binding of vitamin D and cholesterol to beta-lactoglobulin}, volume={80}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(97)76030-2}, abstractNote={Abstract β -Lactoglobulin was isolated directly from acidic whey by bioselective adsorption on N-retinyl-Celite TM , yielding preparations of ≥96% purity. Interactions of these preparations with vitamin D 2 , vitamin D 3 , ergosterol, cholesterol, and 7-dehydrocholesterol were examined by following changes in the fluorescence spectra. Both the excitation and emission spectra indicated that energy was transferred between the tryptophanyl residues of the protein and the chromophore of the ligand. Analyses of the fluorescence changes that occurred upon titration of β -LG with the various ligands allowed determination of the dissociation constant for the complex and the number of moles bound per mole of protein. The affinity for vitamin D 2 (dissociation constant of 4.91 n M ) was 10-fold higher than that of the other compounds, except for ergosterol, which was 5-fold larger than the others. Also, the affinity was 10-fold higher than that typically reported for the retinoids. Furthermore, the value obtained for the number of moles bound per mole of protein was 2 mol·mol –1 for each of the ligands examined in this study; it has been well established that all of the retinoids are bound with a stoichiometry of 1.0. These results suggest that β -LG may be a better carrier of vitamin D than of vitamin A.}, number={6}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QW and Allen, JC and Swaisgood, HE}, year={1997}, month={Jun}, pages={1054–1059} }
 @article{chen_pilkington_tharrington_allen_1997, title={Developing a dry-cured ham nutritional database}, volume={10}, DOI={10.1006/jfca.1997.0534}, abstractNote={Manufacturers of country ham, a dry-cured ham with a minimum 4% NaCl in the finished product, are required by Food Safety and Inspection Service (FSIS) to declare the nutrient content on the label. This study investigated the distribution of nutrients within whole hams to permit calculation of nutrient content for various cuts. Results of a preliminary experiment utilizing six country hams to develop sampling techniques were used to develop the final study protocol. The final study measured the nutrient content of 15 whole hams representative of Southeastern country hams and 7 side meats. Each ham was divided into four sections (butt, center, shank, and hock), which were subdivided into bone and skin, fat, and muscle groups. All muscle and fat samples were analyzed for moisture, protein, fat, sugar profile, cholesterol, fatty acid profile, and minerals (Ca, Fe, K, Na, Zn). Significant variations (P 28% DV), were high in protein and fat (>20% DV), and were “good” to “high” in cholesterol (16 to 28% DV). The lean muscle products contained higher sodium and protein, but lower amounts of fat, cholesterol, and calories compared to untrimmed products. Side meat was higher in calories, fat, and cholesterol but lower in protein and sodium content than country ham products. Country ham products and side meats were low (<2% DV) in total carbohydrate, sugars, and calcium. The data presented for nutrient content of all the muscle systems in whole country hams permit calculations for a nutritional label for virtually all of the subdivided portions of country ham that are currently being marketed.}, number={3}, journal={Journal of Food Composition and Analysis}, author={Chen, H. Y. and Pilkington, D. H. and Tharrington, J. B. and Allen, J. C.}, year={1997}, pages={190–204} }
 @article{heddleson_park_allen_1997, title={Immunogenicity of casein phosphopeptides derived from tryptic hydrolysis of beta-casein}, volume={80}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(97)76140-X}, abstractNote={The immunogenicity of phosphopeptides derived from tryptic hydrolysis of beta-casein (CN) was investigated in a rat model system. The titers of specific immunoglobulin (Ig)G and IgE antibodies made in response to intraperitoneal sensitization to beta-CN, casein phosphopeptides, and skim milk proteins were examined using indirect and amplified indirect ELISA, respectively. Serum IgG antibodies from rats injected with beta-CN were significantly more reactive to beta-CN, casein phosphopeptides, and skim milk proteins coated on microtiter plate wells than were the IgG antibodies generated in rats that had been subjected to other treatments. A significant difference in titers because of the time of sampling (14 or 21 d postinjection) was noted for IgE but not for IgG. Rats that were injected with casein phosphopeptides did not produce IgG antibodies that crossreacted with either skim milk proteins or beta-CN. Specific antibody levels for the IgE class rarely exceeded those of unimmunized controls. The findings suggest that immunogenicity of the phosphopeptides was reduced compared with that of native beta-CN and skim milk proteins.}, number={9}, journal={JOURNAL OF DAIRY SCIENCE}, author={Heddleson, RA and Park, O and Allen, JC}, year={1997}, month={Sep}, pages={1971–1976} }
 @article{heddleson_allen_wang_swaisgood_1997, title={Purity and yield of beta-lactoglobulin isolated by an N-retinyl-Celite bioaffinity column}, volume={45}, ISSN={["0021-8561"]}, DOI={10.1021/jf9605198}, abstractNote={A bioaffinity column of all-trans-retinal immobilized on Celite was capable of isolating high-purity (94.5%) β-lactoglobulin from bovine acid whey. Conditions for producing a potentially hypoallergenic reduced β-lactoglobulin whey were investigated. Reapplication of pH 5.1 eluate to the column resulted in a final purity of 87% α-lactalbumin. The purity of β-lactoglobulin was slightly lower upon elution with buffers containing <0.4 M sodium phosphate, whereas the yield from desorbing buffers <0.1 M decreased to approximately 40% of that obtained with 0.4 M sodium phosphate. Desorption with low phosphate concentration was improved when pH was increased, suggesting that desorption involves titration of a protophilic group on β-lactoglobulin. These findings suggest that the retinal matrix shows promise in its application for creating hypoallergenic products and the isolation of high-purity β-lactoglobulin with useful functional properties. Keywords: β-Lactoglobulin; α-lactalbumin; bioselective adsorption; N-r...}, number={7}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Heddleson, RA and Allen, JC and Wang, QW and Swaisgood, HE}, year={1997}, month={Jul}, pages={2369–2373} }
 @article{allen_vaillancourt_haedrich_1993, title={GLUCOCORTICOID AND POLYAMINE INVOLVEMENT IN ZINC UPTAKE BY COMMA-1D MAMMARY EPITHELIAL-CELLS}, volume={39}, ISSN={["0163-4984"]}, DOI={10.1007/BF02783193}, abstractNote={The objective was to determine if a mammary cell line shows glucocorticoid stimulation of Zn uptake, and to determine whether polyamines mediate this stimulation. 65Zn uptake by COMMA-1D mouse mammary epithelial cells over a 24-h period increased significantly in cells administered 10(-7) or 10(-6) M hydrocortisone. Incorporation of 65Zn over a 1-h period was not hydrocortisone-responsive, suggesting that these incubation times represent uptake into different pools. The rate of entry into the cells over a 15-min period was significantly increased by supplementing cells with hydrocortisone with or without prolactin. Initially, cells grown in lactogenic hormone-supplemented media (10(-6) M hydrocortisone + 5 micrograms/mL ovine prolactin) had up to 65% greater 65Zn uptake over 24 h than cells in nonsupplemented growth media. 65Zn uptake from hormone media with the spermidine synthesis inhibitor methylglyoxal-bis-(guanylhydrazone) (MGBG, 10(-5)M) added was less than from growth media. Exogenous spermidine (10(-6)-10(-3)M) added to the MGBG + hormone media increased 65Zn uptake. Difluoromethylornithine (DFMO), an inhibitor of spermidine synthesis that blocks ornithine decarboxylase, caused a slight dose-dependent decrease in 65Zn uptake over the range 10(-6)-5 x 10(-3)M (p < 0.002) and tended to decrease 65Zn-uptake in lactogenic hormone-stimulated cells with 8 h of incubation, but not at other times. These data show that Zn uptake in mammary epithelial cells can be hormonally mediated by glucocorticoids and suggest that polyamines may be intracellular mediators of this effect.}, number={2-3}, journal={BIOLOGICAL TRACE ELEMENT RESEARCH}, author={ALLEN, JC and VAILLANCOURT, SJ and HAEDRICH, L}, year={1993}, pages={229–243} }
 @article{allen_mascarenhas_1991, title={Effects of a single, pharmacological injection of oxytocin on renal electrolyte clearance in lactating cows}, volume={74}, journal={Journal of Dairy Science}, author={Allen, J. C. and Mascarenhas, K. M.}, year={1991}, pages={223} }