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.
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry