Further Characterization of Earthworm Serine Proteases: Cleavage Specificity Against Peptide Substrates and on Autolysis

Nobuyoshi Nakajima, Manabu Sugimoto, Kohji Ishihara, Kaoru Nakamura, Hiroki Hamada

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    Abstract

    Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-amyloid 1-40 and oxidized insulin B-chain as peptide substrates. The serine protease, F-III-2, cleaved the former substrate at six sites, and the latter at five sites. F-II digested them at six and ten, respectively. The cleavage specificity of F-III-2 resembled those of both trypsin and chymotrypsin. F-II had a broader specificity than F-III-2 and preferred also the bonds consisting neutral or hydrophobic amino acids. Furthermore, F-III-2 itself was digested initially on the site of Arg(144)-Tyr(145) to produce two peptide fragments, when it was autolyzed regularly by heating.

    Original languageEnglish
    Pages (from-to)2031-2033
    Number of pages3
    JournalBioscience, Biotechnology and Biochemistry
    Volume63
    Issue number11
    DOIs
    Publication statusPublished - Jan 1 1999

    Keywords

    • Cleavage specificity
    • Earthworm
    • Fibrinolytic enzyme
    • Serine protease
    • β-amyloid

    ASJC Scopus subject areas

    • Biotechnology
    • Analytical Chemistry
    • Biochemistry
    • Applied Microbiology and Biotechnology
    • Molecular Biology
    • Organic Chemistry

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