
doi: 10.82308/37842
k-Casein which was electrophoretically (Starch gel) homogeneous was hydrolyzed with the enzyme Pronase P and the resultant hydrolyzate was fractionated by column chromatography. A fraction, rich in carbohydrate, was isolated by use of Sephadex G-25. Analysis showed that it contained at least nine different components. Another fraction was isolated by use of Sephadex G-50. Chromatographic, electrophoretic and ultracentrifugal analysis indicated that this fraction contained a single glycopeptide. The glycopeptide contained galactosamine (25.1%), galactose (22.1%) and sialic acid (16.6%), it has no N-term1nal amino acid and has serine as the C-terminal amino acid. Calculation based on the numbers of amino acid residues showed that the molecular weight of the glycopeptide was 11,300. [...]
Baker, B. E. (Supervisor)
Baker, B. (Supervisor)
Agricultural Chemistry., Casein, Agricultural Chemistry
Agricultural Chemistry., Casein, Agricultural Chemistry
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