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 journalArticle

30 Citations (Scopus)


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
Issue number11
Publication statusPublished - Nov 1999



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

ASJC Scopus subject areas

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Bioengineering

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