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Purification and property of extracellular proteases from Vibrio anguillarum(PDF)

Chinese Journal of Applied & Environmental Biology[ISSN:1006-687X/CN:51-1482/Q]

Issue:
Vol.08 No.4
Page:
414-418
Research Field:
Reviews
Publishing date:

Info

Title:
Purification and property of extracellular proteases from Vibrio anguillarum
Author(s):
WEI Yuxiet al.
(Department of Biology, Qingdao University, Qingdao266071, China) (1Institute of Oceanology, Chinese Academy of Sciences, Qingdao266071, China)
Keywords:
Keywords Vibrio anguillarum extracellular product protease
CLC:
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PACS:
DOI:
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DocumentCode:

Abstract:
Abstract The purification and proteolytic activities of extracellular proteases from Vibrio anguillarum isolated from diseased Paralichtys olivaceus were studied. The purification steps included ammonium sulfate precipitation, Sephadex G100 chromatography, DEAESepharose chromatography and DEAECellulose chromatography. Two kinds of proteases were with Mr 37.4×103 and Mr 33.1×103, respectively, but the latter accounted for only a minor fraction of the proteolytic activity for the hydrolysis of azocasein. The Mr 37.4×103 protease was stable and displayed high proteolytic activity in the range of pH 7~10 and 40~60 ℃. It was strongly inhibited by EDTA and 1,10phenanthroline. The result indicated that it was a metalloprotease. Its toxicity to Paralichtys olivaceus is still under way. Fig 6, Tab 3, Ref 17

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Last Update: 2002-10-28