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- W1992574966 abstract "l-Arginase (l-arginine amidinohydrolase, EC 3.5.3.1) was purified in a crystalline form from cells of Bacillus subtilis KY 3281 with an overall yield of 23.2%. The crystalline enzyme had a specific activity of 858 i.u./mg-protein and was ultracentrifugally homogeneous. It was estimated to have a molecular weight of 115,000±5000 by the method of Yphantis. The enzyme highly specific for l-arginine showed the maximum activity at pH 10 with Mn2+ ion. The Km for l-arginine was 1.35 × 10−2 m The activity was competitively inhibited by l-lysine, but not by l-ornithine and increased by the addition of Mn2+ or Co2+ ions. The stable pH and temperature ranges became wider in the presence of Mn2+ ion and l-threonine." @default.
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- W1992574966 date "1973-01-01" @default.
- W1992574966 modified "2023-09-25" @default.
- W1992574966 title "Purification and Properties of L-Arginase from Bacillus subtilis" @default.
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- W1992574966 doi "https://doi.org/10.1271/bbb1961.37.2827" @default.
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