Purification and characterization of an Aeromonas caviae metalloprotease that is related to the Vibrio cholerae hemagglutinin/protease

A zinc metalloprotease (AP34) from Aeromonas caviae was purified by ammoniu m sulfate precipitation and subsequent gel filtration through Sephadex G-10 0 and Sephadex G-50 Superfine. The molecular mass was estimated by sodium d odecyl sulfate-polyacrylamide gel electrophoresis to be 34 kDa. The proteas e showed maximum activity at pH 7.0 and was stable HI 60 degrees C. AP34 wa s completely inactivated by EDTA and Zincov. The N-terminal amino acid sequ ence of AP34 showed a high degree of homology with a range of proteases wit hin 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 a eromonad strains. (C) 1999 Published by Elsevier Science B.V. All rights re served.