SOLUBILITY SOLVATION, AND STABILIZATION OF ALPHAS1-AND BETA-CASEINS

α s1-Casein has been observed to differ from αs1-B by its solubility in CaCl2 solutions at 1 and 37 C, and by its stabilization profile in the presence of κ-casein and calcium ions. The different characteristics of the protein αs1-A have been attributed to the deletion of a segment of nonpolar amino acids resulting in decreased hydrophobic interactions among αs1-A molecules. The deletion also has impaired the formation of αs1-κ-casein micelles under conditions of normal formation. © 1969, American Dairy Science Association. All rights reserved.