Abstract
Radioisotopes were used to show that suspensions of M. leprae oxidized glycerol, phosphogluconate, glucose, G-6-P and, at a low rate, gluconate to CO2. The incubation period in these experiments was usually 20 h, after 140 h, up to 5 times more glucose and gluconate had been converted to CO2. Studies with differentially labeled glucose indicated that glycolysis and the hexose monophosphate pathway were used for glucose dissimilation. Key enzymes of glycolysis, the hexose monophosphate pathway and glycerol catabolism were detected in cell-free extracts from purified M. leprae; phosphoketolase, Entner-Doudoroff pathway activity and gluconate kinase were absent. All these enzymes are also present in host tissue, but biochemical evidence is presented which indicates that all enzymes detected in extracts from M. leprae are authentic bacterial enzymes; they were all detected in extracts of M. leprae prepared by treatment with NaOH in which host enzymes adsorbed to M. leprae were inactivated.
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