Functional Changes of Polyethylene Glycol-modified Serine Proteinase from Aspergillus sojae and Interaction with α_2-Macroglobulin(Biological Chemistry)
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概要
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The covalent attachment of activated polyethylene glycol_2 (PEG2) of 10,000 daltons to nonessential groups on a serine proteinase II (SepII) from Aspergillus sojae produced two modified preparations (PEG_2-SepII-S and PEG_2-SepII-L). The molecular weights of PEG_2-SepII-S and PEG_2-SepII-L were about 170,000 and 280,000, respectively. The PEG_2-SepII-S lost about 80% of its antigenicity, while the PEG_2-SepII-L completely lost its antigenicity. In comparison of kinetic parameters with SepII there was less than 40% variation in Km, but the values of k_<cat> towards succinyl-L-leucyl-L-leucyl-L-valyl-L-tyrosine 4-methylcoumaryl-7-amide (Suc-LLVY-MCA) or succinyl-L-alanyl-L-alanyl-L-valyl-L-alanine p-nitroanilide (Suc-AAVA-pNA) decreased to about 70% less than that of SepII. The modified preparations have about 20% activity towards fibrin hydrolysis and a low affinity for a protein proteinase inhibitor, Streptomyces subtilisin inhibitor (SSI), with a molecular weight of 23,000, while the preparations have high affinity for a low molecular weight microbial inhibitor, chymostatin. The stoichiometry of the reaction of α_2-macroglobulin (α_2M) with PEG_2-SepII-S showed that PEG_2-SepII-L bound to α_2M in a molar ratio of 1:1. No appreciable differences were observed in the pH stabilities of the modified enzymes and the native one at pH 3.6, while the modified enzymes were more stable than that of the native one at pH 11.5. The two modified preparations were labile at 50℃, but the native enzyme was completely stable at 50℃.
- 1989-08-23
著者
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ICHISHIMA EIJI
Department of Bioengineering, Graduate School of Engineering, Soka University
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NAKAJIMA TASUKU
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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Ichishima Eiji
Department Of Bioengineering Graduate School Of Engineering Soka University
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Ichishima E
Department Of Bioengineering Graduate School Of Engineering Soka University
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Ichishima Eiji
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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YAMAGATA Youhei
Department of Agriscience and Bioscience, Tokyo University of Agriculture and Technology
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Nakajima T
Laboratory Of Enzymology Graduate School Of Agricultural Science Tohoku University
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Nakajima Tasuku
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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TAKOI Kiyoshi
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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Yamagata Yukari
Laboratory Of Enzymology Graduate School Of Agricultural Science Tohoku University
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Yamagata Y
Tohoku Univ. Sendai Jpn
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Yamagata Youhei
Dep. Of Applied Molecular Biology And Biochemistry Tokyo Univ. Of Agriculture And Technol.
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Yamagata Youhei
Department Of Applied Molecular Biology And Biochemistry Tokyo University Of Agriculture And Technol
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Yamagata Youhei
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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Ichikawa Eiji
Gekkeikan Research Institute Gekkeikan Sake Co. Ltd.
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Takoi Kiyoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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