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

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

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)47-53
Number of pages7
JournalJournal of Sericultural Science of Japan
Volume69
Issue number1
DOIs
Publication statusPublished - Jan 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

Cite this

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

In: Journal of Sericultural Science of Japan, Vol. 69, No. 1, 01.01.2000, p. 47-53.

Research output: Contribution to journalArticle

Jiang, Yonghuang ; Shirai, Koji ; Okido, Toshihisa ; Banno, Yutaka ; Fujii, Hiroshi. / Purification of 35K protease from the digestive juice of Bombyx mori. In: Journal of Sericultural Science of Japan. 2000 ; Vol. 69, No. 1. pp. 47-53.
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