Abstract
We reported earlier the occurrence of a unique o-diphenoloxidase in Mycobacterium leprae recovered from lepromatous human tissues. No other source of M. leprae fro biochemical studies was available at the time. In the present report, properties of phenoloxidase in M. leprae separated from infected armadillo tissues are presented. The results show that the o-diphenoloxidase remains unaltered in the passage of the bacilli from the human to the the animal host, indicating that the enzyme is an intrinsic characteristic of the leprosy bacteria.
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