Isolation and Identification of λ-Casein

Hydrolysis of αs1-casein by bovine plasmin

“…These products were found (Aimutis and Eigel, 1982) to be analogous to the À-easein fraction previously described in milk (Long et al, 1958;Swaisgood and Brunner, 1961;El Negoumy, 1973).…”

Indigenous enzymes in milk: Overview and historical aspects—Part 1

“…In milk, the principal substrate for plasmin is b-CN, from which it produces g 1 -(b-CN f29-209), g 2 -(b-CN f106-209) and g 3 -(b-CN f108-209) CNs and proteose peptone (PP)5 (b-CN f1-105/107), PP8 slow (b-CN f29-105/107) and PP8 fast (b-CN f1-29). Long, Van Winkle, and Gould (1958) isolated a proteinaceous fraction by ultracentrifugation of a crude k-CN preparation, which they called l-CNs. El-Negoumy (1973) prepared this fraction from milk by ammonium sulphate precipitation in the presence of N,Ndimethyl formamide, and identified by electrophoretic and chromatographic techniques at least nine components with a higher electrophoretic mobility than a S1 -CN.…”

Proteolytic specificity of plasmin on bovine αs1‐Casein

“…yCaseins result from the proteolysis of p-casein by plasmin, the complementary peptides forming part of the proteose peptone fraction of milk (Andrews and Alichanidis, 1983). X.-Casein was described by Long et al (1958), who prepared it from a K-casein preparation by high speed centrifugation. Swaisgood and Brunner (1961) prepared k-casein by fractionating "a-casein" with concentrated trichloroacetic acid-urea.…”