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Starch-gel electrophoretic analysis of the water soluble proteins of pork muscle showed the presence of at least nineteen different components. The fractionation of the water extract by means of acetone precipitation and column chromatography (carboxy-methyl cellulose and Sephadex G-75) led to the isolation of a protein component which was shown by starch-gel electrophoresis and ultra-centrifugation to be homogeneous. The protein had a molecular weight of about 15,500, and the C-terminal amino acid was serine. It showed no esterase or proteolytic activity.
