Purification of 35K protease from the digestive juice of Bombyx mori

Yonghuang Jiang, Koji Shirai, Toshihisa Okido, Yutaka Banno, Hiroshi Fujii

研究成果: ジャーナルへの寄稿記事

5 引用 (Scopus)

抄録

35K protease was purified from the digestive juice of Bombyx mori by a series of chromatography using Butyl-Toyopearl, Sephadex G-50 and DEAE-Sephacel. The purified protease gave a single protein band with a molecular mass of 35,000 on SDS-PAGE and its pi was 9. 1. It had optimal activity at pH11 and in the temperature under 40°C. The enzyme activity was almost completely lost at 60°C and at pH4. It was slightly inhibited by Cu2+and Mn2+, and strongly by diisopropylfluorophosphate, phenylmethylsulfonylfluoride and chymostatin, suggesting that the enzyme may be a chymotrypsin-like protease.

元の言語英語
ページ(範囲)47-53
ページ数7
ジャーナルJournal of Sericultural Science of Japan
69
発行部数1
DOI
出版物ステータス出版済み - 1 1 2000

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digestive juices
Bombyx
Bombyx mori
Purification
Peptide Hydrolases
proteinases
Chymases
Isoflurophate
Enzyme activity
Molecular mass
Enzymes
Chromatography
Polyacrylamide Gel Electrophoresis
chymotrypsin
Temperature
chromatography
enzyme activity
molecular weight
Proteins
enzymes

All Science Journal Classification (ASJC) codes

  • Polymers and Plastics

これを引用

Purification of 35K protease from the digestive juice of Bombyx mori. / Jiang, Yonghuang; Shirai, Koji; Okido, Toshihisa; Banno, Yutaka; Fujii, Hiroshi.

:: Journal of Sericultural Science of Japan, 巻 69, 番号 1, 01.01.2000, p. 47-53.

研究成果: ジャーナルへの寄稿記事

Jiang, Yonghuang ; Shirai, Koji ; Okido, Toshihisa ; Banno, Yutaka ; Fujii, Hiroshi. / Purification of 35K protease from the digestive juice of Bombyx mori. :: Journal of Sericultural Science of Japan. 2000 ; 巻 69, 番号 1. pp. 47-53.
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