Action of rennin on α-, β- and γ-caseins

Abstract

SummaryWhole acid casein and α-, β- and γ-caseins were isolated and treated with rennin. Chemical, chromatographical and electrophoretical analyses were done on the caseins and on the products obtained from them after rennin treatment. Three different fractions were obtained which had some specific protective activity for the Ca-sensitive forms of α-, β- and γ-casein, respectively, and which differed in their chemical, chromatographical, and electrophoretical properties.It is suggested that each casein fraction in milk is associated with its own protective fraction which when released by the action of rennin, allows the casein to clot.

Electrophoresis

“…Pepsinogen (124,378,941,948,1243,1489,1922,2088), streptokinase (520), trypsin (531,976), chymotrvpsin (604); trypsin-inhibiting substances in serum (601,888,1276,2321) and in soybeans (2180); rennin purification (1729) and mode of action (1250,2267,2445), antirennin factor in swine serum (1661)(1662)(1663)(1664)(1665)(1666)(1667)(1668), action of pancreatin on casein (566), isolation of elastases (1415), aspergillus protease (182, 183), B. subtilis protease (1867), bromelin (368); leucine amidopeptidase in human serum (545) and tissue (1595), cattle leucine aminopeptidase (1219), rat aminopeptidases (1538,1724), human serum angiotensinase (1137), human placenta peptidase ( 2482), E. coli mucopeptidases (1738), asparaginase in rat livers (1967,2196), locating asparaginase during continuous electrophoresis (2328);…”