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.
| Original language | English |
|---|---|
| Pages (from-to) | 1854-1861 |
| Number of pages | 8 |
| Journal | Bioscience, biotechnology, and biochemistry |
| Volume | 57 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 1993 |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry