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A hydrophobic interaction site on bovine alpha s1-casein



A hydrophobic interaction site on bovine alpha s1-casein



XXI International Dairy Congress Vol 1, Book 2: 167



Surface hydrophobicity, determined using fluorescent hydrophobic probes and interaction with octyl-Sepharose 4B-CL, was in the order: alpha s1-casein B ( alpha s1-B) > alpha s1-A > alpha s1-I (residues 25-199 of alpha s1-B). Compared with alpha s1-A, alpha s1-B had 13 extra amino acids in positions 14-26.

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