Characterization of the catalase of the genus Porphyromonas isolated from cats

Abstract

Crude cell extracts from members of the genus Porphyromonas isolated from cats were examined in SDS-PAGE and nondenaturing PAGE. In each of the species catalase activity was detected as a single band with characteristics of typical bacterial catalases, i.e. each catalase functioned over a broad pH range (pH 5-10), was not inhibited by chloroform-ethanol, did not possess detectable peroxidase activity, and was irreversibly inhibited by 3-amino-1,2,4 triazole. The catalase enzyme of P. gingivalis VPB 3492, P. circumdentaria NCTC 12469, P. salivosa VPB 3313 and VPB 3444 was inactivated at 71, 66.5, 63.5 and 57 degrees C respectively. The molecular weights of the enzymes from P. gingivalis VPB 3492, P. circumdentaria NCTC 12469, P. salivosa NCTC 11632 and P. salivosa VPB 3444 were 200,000, 216,000, 209,000 and 200,000 Da respectively.