Purification and some properties of chitinase from the stomach of Japanese eel, Anguilla japonica.

• KONO Michiko

  Fisheries Research Laboratory, Faculty of Agriculture, The University of Tokyo

• MATSUI Takashi

  Laboratory of Marine Biochemistry, Faculty of Agriculture, The University of Tokyo

• SHIMIZU Chiaki

  Fisheries Research Laboratory, Faculty of Agriculture, The University of Tokyo

• KOGA Daizo

  Laboratory of Biochemistry, Faculty of Agriculture, Yamaguchi University

抄録

Chitinase (EC 3.2.1.14) was purified from the stomach of Japanese eel, Anguilla japonica, by fractionations with ammonium sulfate, Sephadex G-100 gel filtration, and DEAE-cellulose, CMcellulose, and hydroxylapatite column chromatography. The molecular weight of this enzyme was 50, 000 by SDS-PAGE, and the optimum pH was 4.4. The activity was strongly inhibited by Hg²⁺ and slightly activated by EDTA. The hydrolysis products of colloidal chitin by the enzyme were GlcNAc and GlcNAc₂. When GlcNAc_3-6 was used as substrate, GlcNAc and GlcNAc₂ were recognized as final products with various ratios. GlcNAc₂ was not hydrolyzed by this chitinase.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 54 (4), 973-978, 1990

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390001206462975616
• NII論文ID: 110006324878
• NII書誌ID: AA00515312
• DOI: 10.1271/bbb1961.54.973
• COI: 1:CAS:528:DyaK3cXktF2qs74%3D
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
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  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可