Substrate Specificity of Alkaline Proteases from Cephalosporium sp. KM388
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概要
- 論文の詳細を見る
Serine alkaline proteases from Cephalosporium sp. KM388 were specific against esters of aromatic and hydrophobic amino acids. Against oxidized insulin B-chain, the enzymes initially cleaved the site of Leu-Tyr(15-16). The cleavage specificity of KM388 protease D was broader than those of other alkaline proteases, and the site of Arg-Gly(22-23) was cleaved, which is a specific site for trypsin-like protease.
- 社団法人日本農芸化学会の論文
- 1993-10-23
著者
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Araki T
Faculty Of Bioresources Mie University
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Arai Takamitsu
Faculty Of Bioresources And Center For Molecular Biology And Genetics Mie University
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Aburatani Takeshi
Faculty Of Bioresources Mie University
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TSUCHIYA Katsumi
Faculty of Pharmaceutical Sciences, Josai University
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ARAI Tsutomu
Faculty of Engineering, Toyo University
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Seki K
Chiba Univ. Chiba Jpn
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Seki Kiyohiko
Department Of Applied Biological Sciences Faculty Of Agriculture Saga University
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Arai T
National Inst. Of Fruit Tree Sci. Nagasaki Jpn
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Arai Tsutomu
Faculty Of Engineering Toyo University
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Tsuchiya K
Josai Univ. Saitama Jpn
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SEKI Kazuyuki
Faculty of Pharmaceutical Sciences, Josai University
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Masui Toshinari
Faculty of Pharmaceutical Sciences, Josai University
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Masui Toshinari
Faculty Of Pharmaceutical Sciences Josai University
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Tsuchiya K
Univ. Tokushima Tokushima Jpn
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Tsuchiya Katsumi
Faculty Of Pharmaceutical Sciences Josai University
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Seki Kazuyuki
Faculty Of Pharmaceutical Sciences Josai University
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