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  • Title: Isolation of a low molecular weight active fragment of potato proteinase inhibitor IIb.
    Author: Iwasaki T, Wada J, Kiyohara T, Yoshikawa M.
    Journal: J Biochem; 1975 Dec; 78(6):1267-74. PubMed ID: 5422.
    Abstract:
    A low molecular weight active fragment of potato proteinase inhibitor IIPB was obtained by incubating the inhibitor with an equimolar amount of trypsin [EC 3.4.21.4] at pH 8 and 30 degrees for 16 hr, followed by gel filtration through Sephadex G-50, treatment with trichloroacetic acid, and CM-cellulose chromatography. The purified active fragment consisted of a single peptide chain with a molecular weight of 4,300, comprising 39 amino acid residues. It retained very strong inhibitory activity against chymotrypsin [EC 3.4.21.1] and subtilisin [EC 3.4.21.14]. However, the yield of this active fragment was rather low and was variable. On further incubation with trypsin, it was converted into smaller inactive peptides.
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