Purification and characterization of the mucinase of Vibrio cholerae.

Mucinase from Vibrio cholerae strain CA401 was purified by precipitation with ammonium sulfate and chromatography on a column of BioGel P-100 (Bio-Rad Laboratories, Richmond, California). Ovomucinase, intestinal mucinase, and protease appeared as two peaks of slightly different molecular weights, comigrated in nondenaturing polyacrylamide gel electrophoresis, demonstrated similar patterns of inhibition by heavy metals, and were inhibited by antiserum to purified mucinase. Both molecular weight forms exhibited similar properties, which were identical to those of fresh culture supernatants. Specific activity was only slightly increased by purification. Antiserum to mucinase passively protected infant mice from diarrhea due to V. cholerae.