doi: 10.1093/oxfordjournals.jbchem.a135041.
Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23
- PMID:3888972
- DOI: 10.1093/oxfordjournals.jbchem.a135041
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Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23
H Murai et al. J Biochem.1985 Jan.
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Abstract
Streptomyces Metallo-Proteinase Inhibitor (S-MPI) consists of 102 amino acid residues, including one methionine and two disulfide bridges. The complete amino acid sequence of S-MPI, including two disulfide bridges, was determined by sequencing of tryptic and chymotryptic peptides of two fragments obtained by cyanogen bromide cleavage followed by reduction and S-pyridylethylation of the protein. Incubation of the inhibitor with thermolysin slowly cleaved one peptide bond, Cys(64)-Val(65), which might be a reactive site of S-MPI.