Inhibitory potency of erythrina variegata proteinase inhibitors toward serine proteinases in the blood coagulation and fibrinolytic systems

Tomohiro Nakagaki, Yuko Shibuya, Yoshiaki Kouzuma, Nobuyuki Yamasaki, Makoto Kimura

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

The Erythrina variegata Kunitz family trypsin inhibitors, ETIa and ETIb, prolonged the activated partial thromboplastin time (APTT) and also the prothrombin time (PT) of human plasma, but the Kunitz family chymotrypsin inhibitor, ECI, and Bowman–Birk family inhibitor, EBI, from E. variegata hardly prolonged these times. Trypsin inhibitors ETIa and ETIb inhibited the amidolytic activity of factor Xa, and ETIb but not ETIa inhibited plasma kallikrein. Neither ETIa nor ETIb exhibited any inhibitory activity toward β-factor XIIa and thrombin. Furthermore, trypsin inhibitors ETIa and ETIb inhibited plasmin, a serine proteinase in the fibrinolytic system, whereas ECI and EBI did not. These results indicate that Erythrina Kunitz proteinase inhibitors possess different potency toward serine proteinases in the blood coagulation and fibrinolytic systems, in spite of their high similarity in amino acid sequence.

Original languageEnglish
Pages (from-to)1383-1385
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume60
Issue number8
DOIs
Publication statusPublished - Jan 1996

All Science Journal Classification (ASJC) codes

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

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