The lactic acid oxidase of the mycobacteria.

Edson (1947, 1951), however, pointed out that further purification would be needed before this hypothesis could be tested satisfactorily. A later report showed that the purified enzyme was not a typical flavoprotein (Edson & Cousins, 1953). Since lactate-oxidizing enzymes resembling the enzyme of Myco. phlei have been extracted from Mycobacterium sregmati8, Mycobacterium tuberculo8i8 var. homini8, Mycobacterium tuberculo8i8 var. bovi8 (strain BCG) and Mycobacterium avium (Geronimus, Gray & Birkeland, 1949; Yamamura, Kusunose & Kusunose, 1952; Andrejew, 1954), it is likely that the enzyme is a constituent of all mycobacteria. Its presence in other organisms has not been reported, but a lactic oxidase extracted from Lactobacillus delbruckii is known to require FAD and free riboflavin as cofactors (Hager, Geller & Lipmann, 1954). The purpose of the work described in this paper was to study the properties of the purified enzyme. Of the three species examined Myco. smegmati8 proved to be the richest and most convenient source of the enzyme. After this work was completed Sutton (1954) described an extensive purification of the enzyme extracted from Myco. phlei. MATERIALS AND METHODS