The Complete Amino Acid Sequence of Chitinase-c from the Seeds of Rye (Secale cereal)

Takeshi Yamagami, Gunki Funatsu

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


The complete amino acid sequence of rye seed chitinase-c (RSC-c) has been analyzed. This was done by first sequencing the tryptic peptides from RCm-RSC-c and then connecting them by analyzing the peptides produced by digestions with lysylendopeptidase and Staphylococcus aureus V8 protease of RCm-RSC-c, and by chymotryptic digestion and formic acid cleavage of S. aureus V8 protease peptides. RSC-c consists of 243 amino acid residues and has a molecular mass of 26, 093, and has 92% sequence homology with barley seed basic chitinase which lacks a Cys-rich domain. Cys204 is free and six cysteine residues are linked by disulfide bonds between Cys23 and Cys85, Cys97 and Cys105, and Cys223 and Cys236.

Original languageEnglish
Pages (from-to)1854-1861
Number of pages8
JournalBioscience, biotechnology, and biochemistry
Issue number11
Publication statusPublished - 1993

All Science Journal Classification (ASJC) codes

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


Dive into the research topics of 'The Complete Amino Acid Sequence of Chitinase-c from the Seeds of Rye (Secale cereal)'. Together they form a unique fingerprint.

Cite this