Purification of Primary Structure of Proteinous α-Amylase Inhibitor from Streptomyces chartreusis
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概要
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A new polypeptide inhibitor, AI-409,that inhibits human salivary α-amylase, was purified from a fermentation broth of Streptomyces chartreusis strain No.409. This protein consists of a single-chain polypeptide of 78 amino acid residues, and includes two disulfide bridges. The primary structure of AI-409 and the locations of the disulfide bridges were identified by enzymatic digestion and the automatic Edman technique. Enzymatic digestion was done with trypsin, carboxypeptidase Y, and chymotrypsin. One of the disulfide bridges was between Cys (10) and Cys (26), and the other between Cys (44) and Cys (71).
- 社団法人日本農芸化学会の論文
- 1992-12-23
著者
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SHIMAZU Akira
Institute of Applied Microbiology, The University of Tokyo
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Katsuyama Koichi
Pharmacetuical Research Center Nisshin Flour Milling Co. Ltd.
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IWATA Naohito
Pharmacetuical Research Center, Nisshin Flour Milling Co., Ltd.
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Iwata Naohito
Pharmacetuical Research Center Nisshin Flour Milling Co. Ltd.
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Shimazu Akira
Institute Of Applied Microbiology The University Of Tokyo
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