| Literature DB >> 807522 |
K Prabhakaran, E B Harris, W F Kirchheimer.
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.Entities:
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Year: 1975 PMID: 807522 PMCID: PMC415279 DOI: 10.1128/iai.12.2.267-269.1975
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441