Summary Using polyacrylamide gel electrophoresis, 2-dimensional gel electrophoresis and electrofocusing, it has been shown that 4 basic fragments were produced by action of plasmin on buffalo β-casein. These fragments were present in whole buffalo casein prepared from bulk milk. Their mol. wts, 20000, 16000 and 11000 (2 components) were determined by SDS-gradient polyacrylamide gel electrophoresis. It is suggested that 3 of them are homologous to bovine γ1-, γ2- and γ3-caseins respectively, while the last one (mol. wt 16000), which has no counterpart in plasmin digest of bovine β-casein, could arise from a cleavage at bond 68–69.
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Trieu‐Cuot et al. (1981) studied this question.
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