Identification of the positions of disulfide bonds of chitinase from a marine bacterium, Alteromonas sp. strain O-7.

作者信息

Hayashi K, Sato S, Takano R, Tsujibo H, Orikoshi H, Imada C, Okami Y, Inamori Y, Hara S

机构信息

Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology, Japan.

出版信息

Biosci Biotechnol Biochem. 1995 Oct;59(10):1981-2. doi: 10.1271/bbb.59.1981.

DOI:10.1271/bbb.59.1981

PMID:8534997

Abstract

Extracellular chitinase from marine Alteromonas sp. strain O-7 is unique because of the activation by four major cations contained in sea water, such as Na+, K+, Mg2+, and Ca2+. The positions of S-S bonds of Alteromonas chitinase were identified. Alteromonas chitinase was fragmented by TPCK-trypsin and Staphylococcus aureus V8 protease. The amino acid and sequence analyses of three peptides showed that the positions of disulfide bonds are Cys(94)-Cys(99), Cys(174)-Cys(196), and Cys(386)-Cys(395).

摘要