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Division of Biology, National Research Council of Canada, Ottawa, Ontario
ABSTRACT
One major and two minor para-
-casein components were isolated after rennin treatment from each of two genetic variants of
-casein (A and B) by carboxy-methyl cellulose chromatography. Homocitrullin was present only in the minor components, while the major component was richer in lysine. The minor components were not present in para-
-casein preparations not treated with urea. These findings indicate that the minor para-
-casein components are produced by carbamylation of lysine with the cyanate formed in the urea solution. The homocitrullin-free para-
-caseins A and B were identical as judged by polyacrylamide gel electrophoresis and amino acid analysis. Each contained 108 amino acid residues (molecular weight of about 13,000), and no phosphorus or sialic acid.
2 NRCC Postdoctorate Fellow, 1966–68.
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