01605nas a2200265   4500000000100000008004100001260000900042653001200051653001500063653002100078653002700099653001200126653002500138653003100163653001100194653001200205100001200217700001400229700001100243245005300254300001100307490000700318520100000325022001401325       1978                            d  c197810aAnimals10aArmadillos10aCatechol Oxidase10aDihydroxyphenylalanine10aleprosy10aMycobacterium leprae10aMycobacterium lepraemurium10aSpleen10aTrypsin1 aKim S J1 aIshaque M1 aKato L00aMycobacterium leprae and phenoloxidase activity.  a143-530 v223 a<p>Our earlier studies indicated that the enzyme o-diphenoloxidase was absent in Mycobacterium leprae separated from depromatous human tissues. At that time the bacilli were not available from any other source. The existence or absence of this enzyme in M. leprae recovered from infected armadillo tissues were reinvestigated. The intact cells which were metabolically active, failed to oxidize DOPA. Likewise, DOPA and its derivatives were not oxidized by the enzymatically active cell-free preparations from M. leprae. Upon incubation of DOPA for more than 2 h with whole cell suspensions or particulate fractions, there was no development of colour with an absorption maximum of 540 nm as has been reported for an intermediate of DOPA oxidation. However, DOPA and several phenolic compounds were very actively oxidized by mushroom tyrosinase. The results suggested that M. leprae is deficient in o-diphenoloxidase, and this enzyme is not an intrinsic characteristic of this mycobacterium.</p>  a0026-2633