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  • Title: The complete amino acid sequence of chitinase-c from the seeds of rye (Secale cereal).
    Author: Yamagami T, Funatsu G.
    Journal: Biosci Biotechnol Biochem; 1993 Nov; 57(11):1854-61. PubMed ID: 7764335.
    Abstract:
    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.
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