Open AccessPurification and characterization of an Aeromonas caviae metalloprotease that is related to the Vibrio cholerae hemagglutinin/protease
Author(s) -
Toma Claudia,
Ichinose Yoshio,
Iwanaga Masaaki
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13379.x
Subject(s) - aeromonas caviae , vibrio cholerae , protease , microbiology and biotechnology , ammonium sulfate precipitation , proteases , biology , vibrionaceae , sephadex , gel electrophoresis , polyacrylamide gel electrophoresis , molecular mass , hemagglutinin (influenza) , biochemistry , size exclusion chromatography , bacteria , enzyme , genetics , gene
A zinc metalloprotease (AP34) from Aeromonas caviae was purified by ammonium sulfate precipitation and subsequent gel filtration through Sephadex G‐100 and Sephadex G‐50 Superfine. The molecular mass was estimated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis to be 34 kDa. The protease showed maximum activity at pH 7.0 and was stable at 60° C. AP34 was completely inactivated by EDTA and Zincov. The N‐terminal amino acid sequence of AP34 showed a high degree of homology with a range of proteases within the family Vibrionaceae , including the hemagglutinin/protease (HA/P) of Vibrio cholerae . Immunologic relatedness of AP34 and HA/P was demonstrated by Western blotting. AP34‐like protease was widely distributed among the aeromonad strains.