Positions of disulfide bonds in rye (secale cereale) seed chitinase-a

Takeshi Yamagami, Gunki Funatsu, Masatsune Ishiguro

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2 Citations (Scopus)


The positions of disulfide bonds of rye seed chitinase-a (RSC-a) were identified by the isolation of disulfide-containing peptides produced with enzymatic and/or chemical cleavages of RSC-a, followed by sequencing them. An unequivocal assignment of disulfide bonds in this enzyme was as follows: Cys3-Cys18, Cys12-Cys24, Cys15-Cys42, Cys17-Cys31, and Cys35-Cys39 in the chitin-binding domain (CB domain), Cys82-Cys144, Cys156-Cys164, and Cys282-Cys295 in the catalytic domain (Cat domain), and Cys263 was a free form.

Original languageEnglish
Pages (from-to)1313-1316
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Issue number6
Publication statusPublished - 2000

All Science Journal Classification (ASJC) codes

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


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