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Purification and primary structure of proteinous alpha-amylase inhibitor from Streptomyces chartreusis
K Katsuyama1, N Iwata, A Shimazu
1Pharmaceutical Research Center, Nisshin Flour Milling Co., Ltd., Saitama, Japan.
Bioscience, Biotechnology, and Biochemistry
|December 1, 1992
Abstract:
A new polypeptide inhibitor, AI-409, that inhibits human salivary alpha-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).