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Identification of -Casein as Plasmin-Derived Fragments of Bovine _s1 -Casein

Department of Food Science and Technology, Virginia Polytechnic Institute and State University, Blacksburg 24061

ABSTRACT

Crude -casein, prepared by extraction of whole casein with N,N-di-methylformamide, produced an electrophoretic pattern at pH 9.6 in 4 M urea containing numerous bands with mobilities identical to peptides formed during incubation of _s1-casein with plasmin at 37°C for 10 min. Peptides from two electrophoretic bands were extracted from -casein and were radioiodinated as well as two peptides with identical electrophoretic mobilities from the plasmin digest of _sl -casein. Autoradiograms of tryptic peptide maps from the two peptides extracted from -casein matched peptide maps generated by the corresponding fragments of _s1-casein produced by incubation with plasmin. Sodium dodecyl sulfate gel electrophoretic patterns obtained for the two peptides extracted from -casein were also identical with corresponding peptides extracted after plasmin digestion of _s1-casein. Molecular weights of 5,500 and 6,000 were obtained for the two peptides. The -casein fraction consists predominantly of fragments of _s1-caseins which can be generated in vitro by incubation with bovine plasmin.