RESUMO
Mycobacterium leprae separated from armadillo tissues stored at -80 degrees C is similar to that from human sources in its ability to take up 3H-labelled 3,4-dihydroxyphenylalanine (DOPA). Several inhibitors were studied which showed complete or partial inhibition of [3H]DOPA uptake. These findings suggest that M. leprae isolated from frozen tissue possesses an active uptake system for [3H]DOPA.
Assuntos
Tatus/microbiologia , Di-Hidroxifenilalanina/metabolismo , Mycobacterium leprae/metabolismo , Xenarthra/microbiologia , Animais , Ácido Ascórbico/farmacologia , Quelantes/farmacologia , Baço/microbiologia , TemperaturaRESUMO
Mycobacterium leprae separated from armadillo tissues stored at -80 degrees C is similar to that from human sources in its ability to take up 3H-labelled 3,4-dihydroxyphenylalanine (DOPA). Several inhibitors were studied which showed complete or partial inhibition of [3H]DOPA uptake. These findings suggest that M. leprae isolated from frozen tissue possesses an active uptake system for [3H]DOPA.
Assuntos
Animais , Baço/microbiologia , Xenarthra/microbiologia , Di-Hidroxifenilalanina/metabolismo , Mycobacterium leprae/metabolismo , Quelantes/farmacologia , Tatus/microbiologia , Temperatura , Ácido Ascórbico/farmacologiaRESUMO
Experiments were conducted on the substrate specificity of phenoloxidase in Mycobacterium leprae, by using various phenolic compounds. Comparative studies were carried out with the enzyme from mammalian and plant sources. The phenolase of M. leprae was found to be similar to the enzyme of plant origin in oxidizing a variety of substrates; it was different from the mammalian enzyme, which has a limited substrate specificity. The findings confirmed that phenoloxidase is a specific property of M. leprae and is not a result of adsorption of host-tissue enzymes. The method used in separation of bacilli from infected tissues was evaluated for its effect on the viability of the organisms. This was tested by using M. lepraemurium as a model. The preparative procedure was found to have no adverse effect on the ability of the organisms to multiply in the mouse foot-pad. Several inhibitors of phenoloxidase have been tested-both substrate analogues and compounds which bind copper in the enzyme. Substances binding copper were found to be more effective. Since phenolase has been found to be a characteristic metabolic activity in M. leprae, nontoxic inhibitors of the enzyme offer possibilities of developing a rational chemotherapy of leprosy.