Complete amino acid sequences of three proteinase inhibitors from white sword bean (canavalia gladiata)

Sung Soo Park, Toshihisa Sumi, Hideki Ohba, Osamu Nakamura, Makoto Kimura

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Three major serine proteinase inhibitors (SBI-1, -2, and -3) were purified from the seeds of white sword bean (Canavalia gladiata) by FPLC and reversed-phase HPLC. The sequences of these inhibitors were established by automatic Edman degradation and TOF-mass spectrometry. SBI-1, -2, and -3 consisted of 72, 73, and 75 amino acid residues, with molecular masses of 7806.5, 7919.8, and 8163.4, respectively. The sequences of SBI-1 and -2 coincided with those of CLT I and II [Terada et al. (1994) Biosci. Biotech. Biochem., 58, 376-379] except only N- or C-terminal amino acid residues. Analysis of the amino acid sequences showed that the active sites of the inhibitors contained a Lys21-Ser22 against trypsin and Leu48-Ser49 against chymotrypsin, respectively. Further, it became apparent that about seven disulfide bonds were present. These results suggest that sword bean inhibitors are members of the Bowman-Birk proteinase inhibitor family.

Original languageEnglish
Pages (from-to)2272-2275
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume64
Issue number10
DOIs
Publication statusPublished - 2000

All Science Journal Classification (ASJC) codes

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

Fingerprint Dive into the research topics of 'Complete amino acid sequences of three proteinase inhibitors from white sword bean (canavalia gladiata)'. Together they form a unique fingerprint.

  • Cite this