Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Identification of the Positions of Disulfide Bonds of Chitinase from a Marine Bacterium, Alteromonas sp. Strain O-7
Kaeko HayashiShin-Ichi SatoRyo TakanoHiroshi TsujiboHideyuki OrikoshiChiaki ImadaYoshiro OkamiYoshihiko InamoriSaburo Hara
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JOURNAL FREE ACCESS

1995 Volume 59 Issue 10 Pages 1981-1982

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Abstract

Extracellular chitinase from marine Alteromonas sp. strain 0-7is unique because of the activation by four major cations contained in sea water, such as Na +, K +, Mg 2 +, and Ca 2 + . 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(94FCys(99), Cys(174/Cys(196), and Cys(386/Cys(395).

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© Japan Society for Bioscience, Biotechnology, and Agrochemistry
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