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Phenoloxidase of Mycobacterium leprae [PDF]
Nature, 1967 INVESTIGATIONS of the metabolism of Mycobacteriumleprae1 have revealed a few of the metabolic characteristics of this micro-organism. Concentrates of M. leprae prepared from lepromatous material actively oxidized 3,4-dihydroxyphenylalanine (DOPA) to pigmented products, in vitro2. Among several strains of mycobactena tested (including M. tuberculosis, M.
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Implications of Chemoautotrophism in Mycobacterium leprae
Nature New Biology, 1973Mycobacterium leprae is generally considered as a host-dependent intracellular parasite, deriving energy and nutrients for growth from the human phagocytic cells in which it multiplies abundantly. This has recently been challenged by Kato1,2 who reported that many characteristics of M. leprae recall those of the chemoautotrophic microorganisms.
A. Donawa +3 more
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Protein antigens of Mycobacterium leprae
Research in Microbiology, 1990Protein antigens of Mycobacterium leprae have been identified by screening the lambda gt11, pYA626 and pHC79::M. leprae genomic libraries with pooled sera from leprosy patients and with antiserum to M. leprae cell wall protein (CWP) aggregate. Immunological screening of the lambda gt11 library with pooled sera from 21 lepromatous (LL) leprosy patients ...
E.F. de Carvalho +6 more
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Study on the micromorphology of Mycobacterium leprae
Archives of Dermatological Research, 1985The micromorphology of Mycobacterium leprae is described. After fixation with osmium tetroxide supplemented with calcium ions, the cell wall was seen to be composed of three layers; the cytoplasmic membrane exhibited the architecture of an elementary membrane. The mesosomes were best visualized after fixation with glutaraldehyde; they were sometimes in
G. D. Burchard, M. Bierther
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Properties of Phenoloxidase in Mycobacterium leprae
Nature, 1968Mycobacterium leprae separated from infected human tissues, oxidizes 3,4-dihydroxyphenylalanine (dopa) and a few other phenolic compounds1–3. This property is not shown by several other mycobacteria1,2,4. Phenoloxidase occurs in vertebrate melanocytes and is widely distributed in the plant kingdom5. (E.C.
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