The Complete Amino Acid Sequence of Chitinase-c from the Seeds of Rye (Secale cereal)
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概要
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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.
- 社団法人日本農芸化学会の論文
- 1993-11-23
著者
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Funatsu Gunki
Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric
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YAMAGAMI Takeshi
Laboratories of Protein Chemistry and Engineering
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Yamagami Takeshi
Laboratory Of Protein Chemistry & Engineering Faculty Of Agriculture Kyusyu University
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Funatsu Gunki
Laboratory Of Protein Chemistry & Engineering Faculty Of Agriculture Kyusyu University
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