作者: M.P. Thompson , W.G. Gordon , R.T. Boswell , H.M. Farrell
DOI: 10.3168/JDS.S0022-0302(69)86719-6
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摘要: Abstract α s1 -Casein has been observed to differ from -B by its solubility in CaCl 2 solutions at 1 and 37C, stabilization profile the presence of κ-casein calcium ions. The different characteristics protein -A have attributed deletion a segment nonpolar amino acids resulting decreased hydrophobic interactions among molecules. also impaired formation -κ-casein micelles under conditions normal formation.