Positions of disulfide bonds in rye (secale cereale) seed chitinase-a

Takeshi Yamagami; Gunki Funatsu; Masatsune Ishiguro

doi:10.1271/bbb.64.1313

Positions of disulfide bonds in rye (secale cereale) seed chitinase-a

Takeshi Yamagami, Gunki Funatsu, Masatsune Ishiguro

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

The positions of disulfide bonds of rye seed chitinase-a (RSC-a) were identified by the isolation of disulfide-containing peptides produced with enzymatic and/or chemical cleavages of RSC-a, followed by sequencing them. An unequivocal assignment of disulfide bonds in this enzyme was as follows: Cys3-Cys18, Cys12-Cys24, Cys15-Cys42, Cys17-Cys31, and Cys35-Cys39 in the chitin-binding domain (CB domain), Cys82-Cys144, Cys156-Cys164, and Cys282-Cys295 in the catalytic domain (Cat domain), and Cys263 was a free form.

Original language	English
Pages (from-to)	1313-1316
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	64
Issue number	6
DOIs	https://doi.org/10.1271/bbb.64.1313
Publication status	Published - 2000

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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abstract = "The positions of disulfide bonds of rye seed chitinase-a (RSC-a) were identified by the isolation of disulfide-containing peptides produced with enzymatic and/or chemical cleavages of RSC-a, followed by sequencing them. An unequivocal assignment of disulfide bonds in this enzyme was as follows: Cys3-Cys18, Cys12-Cys24, Cys15-Cys42, Cys17-Cys31, and Cys35-Cys39 in the chitin-binding domain (CB domain), Cys82-Cys144, Cys156-Cys164, and Cys282-Cys295 in the catalytic domain (Cat domain), and Cys263 was a free form.",

author = "Takeshi Yamagami and Gunki Funatsu and Masatsune Ishiguro",

year = "2000",

doi = "10.1271/bbb.64.1313",

language = "English",

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journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

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T1 - Positions of disulfide bonds in rye (secale cereale) seed chitinase-a

AU - Yamagami, Takeshi

AU - Funatsu, Gunki

AU - Ishiguro, Masatsune

PY - 2000

Y1 - 2000

N2 - The positions of disulfide bonds of rye seed chitinase-a (RSC-a) were identified by the isolation of disulfide-containing peptides produced with enzymatic and/or chemical cleavages of RSC-a, followed by sequencing them. An unequivocal assignment of disulfide bonds in this enzyme was as follows: Cys3-Cys18, Cys12-Cys24, Cys15-Cys42, Cys17-Cys31, and Cys35-Cys39 in the chitin-binding domain (CB domain), Cys82-Cys144, Cys156-Cys164, and Cys282-Cys295 in the catalytic domain (Cat domain), and Cys263 was a free form.

AB - The positions of disulfide bonds of rye seed chitinase-a (RSC-a) were identified by the isolation of disulfide-containing peptides produced with enzymatic and/or chemical cleavages of RSC-a, followed by sequencing them. An unequivocal assignment of disulfide bonds in this enzyme was as follows: Cys3-Cys18, Cys12-Cys24, Cys15-Cys42, Cys17-Cys31, and Cys35-Cys39 in the chitin-binding domain (CB domain), Cys82-Cys144, Cys156-Cys164, and Cys282-Cys295 in the catalytic domain (Cat domain), and Cys263 was a free form.

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DO - 10.1271/bbb.64.1313

M3 - Article

C2 - 10923812

AN - SCOPUS:0034198760

SN - 0916-8451

VL - 64

SP - 1313

EP - 1316

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 6

ER -

Positions of disulfide bonds in rye (secale cereale) seed chitinase-a

Abstract

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