Purification and Some Properties of an α-Amylase Inhibitor (Paim) from Streptomyces corchorushii
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概要
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Paim, a microbial animal amylase inhibitor, was purified from the culture filtrate of Streptomyces corchorushii by salting out with ammonium sulfate and column chromatography on DEAE-cellulose, TEAE-cellulose, SP-Sephadex C-50, and Octyl Sepharose CL-4B. Paim was separated into 2 fractions (Paim I and II), both homogeneous on disc electrophoresis. The molecular weight of Paim I was 4100 and that of II, 4400 by amino acid analysis. Paim I and II consisted of 39 and 42 amino acid residues, respectively, and contained no lysine, isolecucine, or phenylalanine. Paim contained no carbohydrate moiety, and was stable even after being treated at 100°C for 10min in the pH range from 5 to 8.
- 社団法人 日本農芸化学会の論文
著者
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Arai Motoo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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OOUCHI Naoki
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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