Purification and Some Properties of an Esterase from Yeast
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概要
- 論文の詳細を見る
An esterase was isolated and purified from baker's yeast by ammonium sulfate precipitation and column chromatographies on Sephacryl S-200,DEAE-Sephacel, chromatofocusing, and DEAE-Sephacel again. The molecular weight of the enzyme was approximately 84,000 on Sephadex G-100 and 40,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting a dimer for the activity. This enzyme hydrolyzed short-chain naphthyl esters and p-nitrophenyl esters, and its activity was strongly inhibited by mercuric compounds. The esterase appeared to be an arylesterase (EC 3.1.1.2) and its optimum pH was 8.0 at 30℃.
- 公益社団法人日本生物工学会の論文
- 1986-10-25
著者
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Kojima M
Faculty Of Pharmaceutical Sciences Fukuoka University
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Kojima Misao
Faculty Of Pharmaceutical Sciences Fukuoka University
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Hamada H
Faculty Of Pharmaceutical Sciences Fukuoka University
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Hamada Hiroshi
Faculty Of Engineering Okayama University
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TOSHIMITSU NORIKO
Faculty of Pharmaceutical Sciences, Fukuoka University
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Toshimitsu Noriko
Faculty Of Pharmaceutical Sciences Fukuoka University
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