Preparation and Some Properties of Active Monomer of Sweet Potato β-Amylase(Biological Chemistry)
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概要
- 論文の詳細を見る
Sweet potato β-amylase was divided into two active fractions (named F-A and F-B) by modification with periodate-oxidized maltohexaose at pH 9.7. F-A and F-B isolated by exclusion chromatography using Sephadex G-200 corresponded to a pentamer of the enzyme with molecular weight of 31.5×10^4 and a monomer with molecular weight of 6.4×10^4, respectively. The contents of carbohydrate of the modified enzymes were 9.7% for F-A and 9.3% for F-B. The specific activities of F-A and F-B were 2,059 and 1,129 units/mg of protein and were reduced to 82% and 45% of that of the original enzyme, respectively. The modification of the enzyme with the oxidized maltohexaose was due to formation of a Schiff base between ε-NH_2 groups of lysines of the enzyme protein and CHO groups of the oxidized maltohexaose.
- 社団法人日本農芸化学会の論文
- 1990-03-23
著者
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YAMAMOTO Takehiko
Faculty of Engineering, Fukuyama University
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MINAMIURA Noshi
Faculty of Science, Osaka City University
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Ann Y‐g
Osaka City Univ. Osaka Jpn
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Iizuka Masaru
Faculty Of Science Osaka City University
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Iizuka Masaru
Department Of Bio- And Geo-science Graduate School Of Science Osaka City University
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Yamamoto T
Novelty Materials Research Institute Hannan R&d Center Fuji Oil Co.ltd.
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Minamiura N
Department Of Bio- And Geo-science Graduate School Of Science Osaka City University
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Minamiura Noshi
Faculty Of Science Osaka City University
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Iizuka M
Department Of Bio- And Geo-science Graduate School Of Science Osaka City University
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ANN Yong-Geun
Faculty o f Science, Osaka City University
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Yamamoto T
Department Of Biotechnology Fukuyama University
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Yamamoto Takehiko
Faculty Of Engineering Fukuyama University
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