Purification and Characterization of N-Acetylmuramyl-L-alanine Amidase from Streptomyces globisporus 1829
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概要
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The enzyme, N-acetylmuramyl-L-alanine amidase (mucopeptide aminohydrolase EC 3.5. 1. 18) was found in mutanolysin, which was purified partially from the cultural broth of Streptomyces globisporus 1829. This enzyme was highly purified. The overall purification was 37.5-fold with a yield of 19.2% from mutanolysin. The molecular weight of the enzyme was 18, 500 as determined by plate gel filtration. The enzyme was inhibited by Cu++. This enzyme has a preference for substances of lower molecular weight and seems to be dependent on the prior action of a hexosamidase. This enzyme is not bacteriolytic per se.
- 社団法人 日本農芸化学会の論文
著者
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YOKOGAWA Kanae
Research Laboratory, Dainippon Pharmaceutical Co., Ltd.
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Kawata Shigeo
Research Information Center Institute Of Plasma Physics Nagoya University
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TAKASE Yoshiyuki
Research Laboratories, Dainippon Pharmaceutical Co., Ltd.
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TAKEMURA Tadashi
Research Laboratories, Dainippon Pharmaceutical Co., Ltd.
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TAKEMURA Tadashi
Research Laboratories, Dainippon Pharmaceutical Co.
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YOKOGAWA Kanae
Research Laboratories, Dainippon Pharmaceutical Co.
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