@article{jang_swaisgood_1990, title={ANALYSIS OF LIGAND-BINDING AND BETA-LACTOGLOBULIN DENATURATION BY CHROMATOGRAPHY ON IMMOBILIZED TRANS-RETINAL}, volume={73}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(90)78886-8}, abstractNote={Abstract The possibility of using biorecognition as an indicator of native structure in β-lactoglobulin was investigated with an immobilized analog of retinal. Trans -retinal was covalently bound to 200-nm pore diameter aminopropyl-controlled-pore glass by reductive amination with sodium cyanoborohydride. The immobilized trans -retinal was packed into a 3-mm x 150-mm glass column and incorporated into an HPLC unit. Using continuous elution analytical affinity chromatography, the measured dissociation constant is 35.6 nM, which is similar to the value reported for binding of retinol to β-lactoglobulin in solution. Thus, the nonpolar portion of the ligand is largely responsible for binding as previously suggested. Zonal chromatography of β-lactoglobulin and α-lactalbumin mixtures or whey samples resulted in rapid separation of native β-lactoglobulin from the denatured form and all other proteins. Samples containing varying quantities of native and denatured protein were prepared by heat treatment. Analyses of these samples for the amount of native β-lactoglobulin by chromatography were compared to literature values obtained from solubility measurements. The two methods are in excellent agreement.}, number={8}, journal={JOURNAL OF DAIRY SCIENCE}, author={JANG, HD and SWAISGOOD, HE}, year={1990}, month={Aug}, pages={2067–2074} }
 @article{jang_swaisgood_1990, title={Disulfide bond formation between thermally denatured beta-lactoglobulin and kappa-casein in casein micelles}, volume={73}, DOI={10.3168/jds.s0022-0302(90)78746-2}, abstractNote={Abstract Interaction between thermally denatured β-lactoglobulin and κ-casein has been suggested to occur via a sulfhydryl-disulfide interchange leading to an intermolecular disulfide bond. Direct evidence for a sulfhydryl-disulfide interchange between β-lactoglobulin and κ-casein in native casein micelles was obtained by heat treatment of native micelles, obtained and used immediately without exposure to temperature below 20°C, in the presence of β-lactoglobulin that was covalently immobilized on 3000-A pore diameter porous glass beads. Washing the beads with low pH urea solutions removed all non-covalently bound proteins without further interchange. Treatment of the washed beads with a reducing agent released protein attached through disulfide bonds which was then identified by PAGE. Only κ-casein could be identified in the reductively released protein. No reductively released protein could be detected in samples treated at 55 or 65°C. A small amount of κ-casein was present in the reductive eluant following heat treatment at 75°C; however, a much greater amount was attached through intermolecular disulfide bonds when the mixture was heated at 85°C.}, number={4}, journal={Journal of Dairy Science}, author={Jang, H. D. and Swaisgood, H. E.}, year={1990}, pages={900} }
 @article{jang_swaisgood_1990, title={Interaction of calcium with casein submicelles}, volume={73}, journal={Journal of Dairy Science}, author={Jang, H. D. and Swaisgood, H. E.}, year={1990}, pages={106} }