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Original Articles

Positions of Disulfide Bonds in Rye (Secale cereale) Seed Chitinase-a

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Pages 1313-1316 | Received 13 Dec 1999, Accepted 21 Jan 2000, Published online: 22 May 2014
 

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.

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