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- W2046289032 abstract "Three types of proteinases contained in baker's yeast were fractionated and partially purified by chromatography on TEAE-cellulose and on DEAE-Sephadex. These enzymes were designated as proteinase A, B and C, and some properties of proteinase A and B were described. A was similar to pepsin and “acid-proteinase” produced by various fungi, but did not hydrolyze carbobenzoxy-L-glutamyl-L-tyrosine. B had milk-clotting activity and proteolytic activity toward casein, and also esterolytic activity toward N-acetyl-L-tyrosine ethylester and α-N-benzoyl-L-arginine ethylester. This enzyme was inhibited by p-mercuribenzoate and diisopropylphosphorofluoridate." @default.
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- W2046289032 date "1967-01-01" @default.
- W2046289032 modified "2023-10-17" @default.
- W2046289032 title "Purification of Yeast Proteinases" @default.
- W2046289032 doi "https://doi.org/10.1271/bbb1961.31.150" @default.
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