Purification and Properties of l-Arginase from Bacillus subtilis |
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Authors: | Nobuo Nakamura Masako Fujita Kazuo Kimura |
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Affiliation: | Kyowa Hakko Kogyo Co., Ltd., Tokyo Research Laboratory Asahi-machi, Machida, Tokyo |
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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. |
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