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Purification of Protease from Vibrio cholerae O1 and its Partial Characterization

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Title: Purification of Protease from Vibrio cholerae O1 and its Partial Characterization
Authors: Ichinose, Yoshio / Ehara, Masahiko / Utsunomiya, Akiyoshi
Issue Date: 30-Sep-1992
Publisher: 長崎大学熱帯医学研究所 / Institute of Tropical Medicine, Nagasaki University
Citation: 熱帯医学 Tropical medicine 34(3). p121-125, 1992
Abstract: A protease produced by a clinical isolate of Vibrio cholerae O1 was purified to apparent homogeneity by ammonium sulfate fractionation, ultracentrifuge and succesive column chromatography on a Bio-gel A5m and a TSK gel G-3000SW HPLC column. The molecular weight of the purified protease was estimated to be 32,000 on the basis of its mobility on SDS-PAGE and was identical to HA/protease biochemically and physicochemically as previously reported (Booth et al., 1983; Honda et al., 1987). The hemagglutinin activity of purified protease, however, was not detected as previously described. The purified protease seemed to be identical biochemically and physicochemically but did not show the character of a bifunctional protein molecule.
URI: http://hdl.handle.net/10069/4605
ISSN: 03855643
Type: Departmental Bulletin Paper
Appears in Collections:Volume 34, No. 3

Citable URI : http://hdl.handle.net/10069/4605

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