Isolation and Characterization of Catalase Produced byMycobacterium tuberculosis1

Publisher Website
Google Scholar
Abstract
Catalase derived from M. tuberculosis was purified by ammonium sulfate precipitation, ion exchange chromatography, and gel filtration. This product has a molecular weight of about 160,000, exhibits a peak absorption in the Soret band, and gives a positive reaction with benzidine. It has peroxidase-like activity at pH 7.5 but not at 4.0. Inactivation of the catalase by isoniazid or its isomer, nicotinic acid hydrazide, is intensified by cupric ion. Phosphate can protect the pure enzyme from the deleterious effect of isoniazid, and dialysis of isoniazid-inactivated catalase results in partial restoration of its activity. 3-Amino-1,2,4-triazole stimulates M. tuberculosis catalase activity, in contrast to its inhibitory effect on catalase from some other sources.

This publication has 0 references indexed in Scilit: