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- W1992907732 abstract "Lysozyme (mucopeptide N-acetyhmiramylhydrolase, EC 3.2.1.17) (murami-dase) has been purified from fresh raw bovine milk. The method involved separation of whole milk to obtain skim milk, preparation of the acid whey from the skim milk, adsorption of lysozyme from the whey onto Amberlite IRC-50, fractional precipitation with ammonium sulfate, and then twice chromatographing on Sephadex G-50. The isolated enzyme showed a purification of 36 000-fold on a milk protein basis and a specific activity of 0.35 in comparison with 1.0 for egg-white lysozyme. Starch gel electrophoresis and sedimentation behavior of the enzyme preparation indicated it to be homogeneous. The isolated enzyme protein seemed to have an isoelectric point of pH 9,5 and apparently possessed a molecular weight similar to that of egg-white lysozyme. The purified enzyme in 0.067 M phosphate buffer displayed a pH optimum of 7.9. The enzyme required salts for activity; sodium citrate was the most potent activator of the enzyme activity." @default.
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- W1992907732 date "1965-01-01" @default.
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- W1992907732 title "Purification and some properties of bovine milk lysozyme" @default.
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- W1992907732 doi "https://doi.org/10.1016/s0926-6593(65)80046-7" @default.
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