Purification and Some Properties of Achromobacter Protease Ia from Achromobacter lyticus M497-1(Biological Chemistry)
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概要
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A protease with strict specificity to lysyl peptide bonds like that of Achromobacter protease I was purified from a crude enzyme powder obtained from a culture filtrate of Achromobacter lyticus M497-1 and characterized. The purified enzyme had the following differences from protease I.. The enzyme had an isoelectric point of 5.3, lower than the value of 6.9 for protease I. The amino acid composition of the enzyme had higher proportions of His, Glu, and Gly and lower proportions of Arg and Thr than protease I. The enzyme was unstable (30% residual activity) in the presence of 7M urea (pH 8.0, 30℃, 20min); oritease I was resistant to the same conditions (80% residual activity). The k_<cat>/Km values for the hydrolysis of Tos-Lys-Ome and Lys-pNA by the enzyme were lower than those of prtease I.
- 社団法人日本農芸化学会の論文
- 1986-12-23
著者
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Masaki Takeharu
Department of Resource Biology, Faculty of Agriculture, Ibaraki University
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Soejima Masami
Department of Resource Biology, Faculty of Agriculture, Ibaraki University
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Suzuki H
Kitasato Univ. School Of Medicine Kanagawa Jpn
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Masaki Takeharu
Department Of Agricultural Chemistry Faculty Of Agriculture Ibaraki University
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SUZUKI Hideya
Department of Agricultural Chemistry, Faculty of Agriculture, Ibaraki University
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Soejima Masami
Department Of Agricultural Chemistry Faculty Of Agriculture Ibaraki University
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Suzuki Hideya
Department Of Agricultural Chemistry Faculty Of Agriculture Ibaraki University
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