Hayashi K, Sato S, Takano R, Tsujibo H, Orikoshi H, Imada C, Okami Y, Inamori Y, Hara S
Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology, Japan.
Biosci Biotechnol Biochem. 1995 Oct;59(10):1981-2. doi: 10.1271/bbb.59.1981.
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).
来自海洋交替单胞菌属O-7菌株的胞外几丁质酶很独特，因为它能被海水中所含的四种主要阳离子（如Na+、K+、Mg2+和Ca2+）激活。已确定交替单胞菌几丁质酶的二硫键位置。交替单胞菌几丁质酶用TPCK-胰蛋白酶和金黄色葡萄球菌V8蛋白酶进行了切割。对三个肽段的氨基酸和序列分析表明，二硫键的位置为Cys(94)-Cys(99)、Cys(174)-Cys(196)和Cys(386)-Cys(395)。
