Purification, Crystallization and Some Properties of β-Cyano-L-alanine-degrading Enzyme in Pseudomonas sp. 13
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概要
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A β-cyano-L-alanine (β-CNAla)-degrading enzyme in Pseudomonas sp. 13 was purified and isolated as a crystalline preparation. The purification procedure involved ethanol fractionation, ammonium sulfate fractionation, column chromatography on DEAE-cellulose and crystallization in the presence of ammonium sulfate, resulting in 660-fold purification with a yield of 21%. The crystalline enzyme was homogeneous as judged by ultracentrifugation and SDS-polyacrylamide gel electrophoresis. The enzyme has a molecular weight of approximately 1, 000, 000, and consists of about 30 apparently identical subunits, each of a molecular weight of approximately 35, 000. The enzyme catalyzed the hydrolysis of β-CNAla to form asparagine and aspartic acid. The enzyme reaction was inhibited strongly by thiol reagents.
- 社団法人 日本農芸化学会の論文
著者
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Yanase Hideshi
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Sakai Takuo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Tonomura Kenzo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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