Improved Purification and Further Characterization of Acid Carboxypeptidase from Aspergillus saitoi(Biological Chemistry)
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概要
- 論文の詳細を見る
An acid carboxypeptidase was highly purified and characterized from Aspergillus saitoi ATCC 14332. By disc gel electrophoresis at pH 9.4, SDS disc gel electrophoresis, and isoelectric focusing, the enzyme was essentially homogeneous. The molecular weight was 125,000 by gel filtration and 72,000 by SDS disc gel electrophoresis. The isoelectric point was 4.07. The enzyme acted as a carboxyamidase for cholecystokinin-tetrapeptide (CCK-tetrapeptide, Trp-Met-Asp-Phe-NH_2). The Km and k_<cat> values of the enzyme for Z-Glu-Tyr, angiotensin, and bradykinin at pH 3.1 and 30℃ were 4.0mM and 106sec^<-1>, 0.05mM and 0.35sec^<-1>, and 0.04mM and 6.0sec^<-1>, respectively. An aqueous solution of the enzyme was freeze-dried retaining 98% of the enzyme activity. None of the activity was lost after preservation for 3 years at 4℃.
- 社団法人日本農芸化学会の論文
- 1986-06-23
著者
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ICHISHIMA Eiji
Laboratory of molecular Enzymology, Department of Applied Biological Chemistry, Faculty of Agricultu
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Ichishima E
Tohoku Univ. Sendai Jpn
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TAKEUCHI Michio
Laboratory Enzymology and Microbial Chemistry, Tokyo University of Agriculture and Technology
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Takeuchi M
Research Institute Nihon Shokuhin Kako Co. Ltd.
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Takeuchi Masayoshi
Department Of Biological Chemistry School Of Pharmacy Hokuriku University
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Takeuchi Michio
Laboratory Enzymology And Microbial Chemistry Tokyo University Of Agriculture And Technology
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Ichishima Eiji
Laboratory Of Enzymology And Microbial Chemistry Tokyo Noko University
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