THE SEQUENCE OF THE ALPHA-AMYLASE INHIBITOR HOE-467-A (ALPHA-AMYLASE INACTIVATOR HOE-467-A) FROM STREPTOMYCES-TENDAE 4158

  • 1 January 1981
    • journal article
    • research article
    • Vol. 362  (4) , 465-467
Abstract
An .alpha.-amylase inhibitor isolated from S. tendae strain 4158 was repurified by chromatography on CM[carboxymethylcellulose]- and DEAE-cellulose column. Two inhibitors could be characterized: .alpha.-amylase inhibitor Hoe 467A (with Asp as N-terminal residue), and .alpha.-amylase inhibitor Hoe 467S (with Ser as N-terminal residue). The primary structure was determined by automatic Edman-degradation procedures of the aziranized inhibitor and tryptic peptides, derived from digestions of the performic oxidized, aziranized and maleylated inhibitor, respectively. The .alpha.-amylase inhibitor Hoe 467A consists of 74 residues and has a calculated MW of 7958. It is composed of all of the common amino acids except for methionine and phenylalanine. Digestion with pepsin was performed to determine whether disulfide bonds were present. Two fractions could be isolated, containing one cystine each giving information about the position of the disulfide bridges. The possible clinical application of the inactivator in diabetes mellitus is discussed.

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