Literature DB >> 7764335

The complete amino acid sequence of chitinase-c from the seeds of rye (Secale cereal).

T Yamagami1, G Funatsu.   

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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Year:  1993        PMID: 7764335     DOI: 10.1271/bbb.57.1854

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  1 in total

1.  Chitinase genes responsive to cold encode antifreeze proteins in winter cereals.

Authors:  S Yeh; B A Moffatt; M Griffith; F Xiong; D S Yang; S B Wiseman; F Sarhan; J Danyluk; Y Q Xue; C L Hew; A Doherty-Kirby; G Lajoie
Journal:  Plant Physiol       Date:  2000-11       Impact factor: 8.340

  1 in total

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