@article{wilcox_janolino_swaisgood_2002, title={Isolation and partial characterization of CD36 from skim milk}, volume={85}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(02)74265-3}, abstractNote={CD36, a common milk fat globule membrane glycoprotein, was isolated from skim milk by methods similar to those previously utilized for the isolation of sulfhydryl oxidase. Two separate methods that were employed, gave similar purity as observed by electrophoresis. The first was based on differential centrifugation and size-exclusion chromatography, whereas the second combined ultrafiltration and affinity chromatography. After significant purification, the protein was identified by Western blotting and sequence analysis. Deglycosylation decreased the apparent molecular mass from approximately 85 to 57 kDa. These results suggested tissue-specific glycosylation. The purified fractions also exhibited low levels of sulfhydryl oxidase activity, the significance of which will require further study.}, number={8}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wilcox, CP and Janolino, VG and Swaisgood, HE}, year={2002}, month={Aug}, pages={1903–1908} }
 @article{janolino_swaisgood_2002, title={Trypsin imobilization on derivatized cellulose beads by biospecific avidin-biotin interaction and characterization of the immobilized activity}, volume={26}, DOI={10.1111/j.1745-4514.2002.tb00869.x}, abstractNote={Trypsin was immobilized on cellulose beads using the biospecific and high affinity avidin-biotin interaction. Trypsin and cellulose beads were biotinylated with sulfosuccinimidyl-6-(biotinamido) hexanoate (NHS-LC-biotin). Avidin and biotinylated trypsin were sequentially adsorbed to the biotinylated cellulose beads. A similar procedure was carried out using controlled-pore glass (CPG) beads. The properties of the two trypsin bioreactors were examined and compared. The substrate used for the assay of trypsin activity was p-tosyl-L-arginine methyl ester and the extent of biotinylation of biotinylated trypsin and of immobilized biotin on cellulose beads and on CPG beads were determined using the 2-[4'-hydroxyazobenzene]benzoic acid dye-binding method. Biotinylated trypsin in solution retained about 82% of the specific activity of native trypsin. Cellulose beads contained 0.184 μmol/mL (1.15 μmol/g) biotin and CPG beads, 0.329 μmol/mL (0.987 μmol/g). After regeneration, the biotin contents became slightly lower, namely, 0.159 μmol/mL for cellulose beads and 0.315 μmol/mL for CPG beads. The specific activities of trypsin immobilized on cellulose beads and CPG beads were 32 U/mL (202 U/g) and 43 U/mL (130 U/g), respectively. These studies indicate that cellulose beads can be biotinylated for use as bioselective support. Cette etude utilise l'interaction avidine-biotine comme modele pour l'adsorption selective et l'immobilisation de proteines de fusion enzyme-streptavidine recombinantes pour la preparation de bioreacteur. L'application de cette technologie permet de realiser la purification et l'immobilisation dans une seule etape. Cette etude caracterise enfin la trypsine immobilisee par cette methode en comparaison avec celle immobilisee sur des billes de verre.}, number={2}, journal={Journal of Food Biochemistry}, author={Janolino, V. G. and Swaisgood, H. E.}, year={2002}, pages={119–129} }
 @article{janolino_swaisgood_1992, title={A comparison of sulfhydryl oxidases from bovine milk and from Aspergillus niger}, volume={47}, number={3}, journal={Milchwissenschaft [Milk Science International]}, author={Janolino, V. G. and Swaisgood, H. E.}, year={1992}, pages={143} }
 @article{janolino_morrisonrowe_swaisgood_1990, title={CONFIRMATION OF A BLOCKED AMINO TERMINUS OF SULFHYDRYL OXIDASE}, volume={73}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(90)78909-6}, abstractNote={The isolation of sulfhydryl oxidase from bovine milk in a suitably pure form for sequencing was carried out by transient covalent affinity chromatography of diafiltered whey using cysteinylsuccinamidopropyl-glass as matrix. The glutathione-eluted proteins were separated by SDS-PAGE. By radiolabeling the affinity chromatography-purified enzyme with [14C]iodoacetate before subjecting to SDS-PAGE, the sulfhydryl oxidase band was identified, because sulfhydryl oxidase is known to be inactivated by alkylation of one sulfhydryl group per mole. The results confirmed that sulfhydryl oxidase corresponds to the 85 (+/- 5)-k-Daband observed on SDS-PAGE. The protein band corresponding to radiolabeled sulfhydryl oxidase was recovered from SDS-PAGE gels by electrophoretic elution and by electroblotting on polyvinylidene difluoride membrane and polyvinylidene difluoride membrane and subjected to gas phase sequencing. Precautions were taken during electrophoretic elution to prevent reactions that result in N-terminal blocking. Both methods of protein recovery yielded negative results when subjected to sequence analysis indicating that the N-terminus of sulfhydryl oxidase is blocked.}, number={9}, journal={JOURNAL OF DAIRY SCIENCE}, author={JANOLINO, VG and MORRISONROWE, SJ and SWAISGOOD, HE}, year={1990}, month={Sep}, pages={2287–2291} }
 @article{janolino_swaisgood_1990, title={HOMOGENEITY OF SULFHYDRYL OXIDASE PREPARATIONS OBTAINED BY TRANSIENT COVALENT AFFINITY-CHROMATOGRAPHY}, volume={73}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(90)78674-2}, abstractNote={Abstract Bovine milk sulfhydryl oxidase was prepared by transient covalent affinity chromatography on a cysteinylsuccinamidopropyl glass matrix. The homogeneity of this preparation was examined by immunofixation electrofocusing, SDS-PAGE, and size exclusion chromatography in 6 M guanidinium chloride. The major contaminant of this preparation, prepared from whey diafiltered with a 1000 kdal exclusion limit membrane, was IgG. Immunoglobulin M could not be detected. Presence of IgG in these sulfhydryl oxidase preparations suggests an interaction between IgG and either skim milk membrane vesicles or sulfhydryl oxidase.}, number={2}, journal={JOURNAL OF DAIRY SCIENCE}, author={JANOLINO, VG and SWAISGOOD, HE}, year={1990}, month={Feb}, pages={308–313} }
 @article{janolino_swaisgood_1989, title={Sequencing studies of the active site tryptic peptide of sulfhydryl oxidase}, volume={72}, journal={Journal of Dairy Science}, author={Janolino, V. G. and Swaisgood, H. E.}, year={1989}, pages={174} }