Database : HANSEN
Search on : PEROXIDASES/METAB [Subject descriptor]
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Id:13487
Author:McKeever, Paul E; Walsh, Gerald P; Storrs, Eleanor E; Balentine, J. Douglas
Title:Electron microscopy of peroxidase and acid phosphatase in leprous and uninfected armadillo macrophages: a macrophage subpopulation contains peroxisomes and lacks bacilli ..-
Source:s.l; s.n; sep. 1978. 11 p. ilus.
Abstract:Lepromatous tissue from armadillos inoculated 24--36 months earlier with Mycobacterium leprae was obtained for electron microscopic studies. Cytochemically stained lepromas revealed a subpopulation of macrophages containing peroxisomes. These peroxidase reactive macrophages were not infected with bacilli. Acid phosphatase was present in macrophages and many of these were infected with bacilli and contained vacuoles and lipid globules. Within the membrane-bound vacuoles, acid phosphatase surrounded bacilli. However, the reaction product ended abruptly at a 15--40 millimicron thick zone of low electron density surrounding intact bacilli. Acid phosphatase was more intensely reactive and localized less precisely in heavily infected and vacuolated macrophages than in lightly and non-infected cells. The effectiveness of this bacillary barrier and the numerous infected macrophages with substantial acid phosphatase argue against the ability of acid phosphatase to protect host cells from leprosy bacilli. Evidence suggests a protective action of peroxidase or the rapid turnover of macrophages within lepromas. Granular and membranous debris were commonly seen within vacuoles of infected macrophages. A portion of the debris was ultrastructurally similar to bacillary matrix and was nonreactive for peroxidase and acid phosphatase. Following homogenization and centrifugation, similar materials banded with bacilli above 60% sucrose. Another portion of the debris was ultrastructurally similar to host lysosomal matrix and was reactive for acid phosphatase. Results support the concept of dual host and parasitic origins of the debris found in phagolysosomes of infected macrophages. Transparent, oval Epon defects remained eccentric to the majority of intact bacilli in centrifuged fractions. Apparently, an intrinsic property of leprosy produced these Epon defects.(AU).
Descriptors:PEROXIDASES/metab
HISTOCITOQUIMICA
MODELOS ANIMAIS DE DOENCAS
MYCOBACTERIUM LEPRAE/isol
MACROFAGOS/enzimol
MACROFAGOS/microbiol
HANSENIASE/enzimol
HANSENIASE/microbiol
Limits:ESTUDO COMPARATIVO
ANIMAL
SUPPORT, U.S. GOV'T, P.H.S.
FOSFATASE ACIDA/*ME
TATUS
Electronic Medium:http://www.ilsl.br
Location:BR191.1; 1307/s


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Id:12309
Author:Kang, Tae-Jin; You, Ji-Chang; Chae, Gue-Tae
Title:Identification of catalase-like activity from mucobacterium leprae and the relationship between catalase and isonicotinic acid hydrazide (INH) ..-
Source:s.l; s.n; 2001. 7 p. ilus, tab, graf.
Descriptors:SULFATO DE AMONIO
ANTITUBERCULOSOS
SEQUENCIA DE BASES
BENZIDINAS
CATALASE
CATALASE
PRIMERS DO DNA
DNA COMPLEMENTAR
ELETROFORESE EM GEL DE AGAR
PEROXIDO DE HIDROGENIO
ISONIAZIDA
HANSENIASE
HANSENIASE
MACROFAGOS PERITONEAIS
CAMUNDONGOS
CAMUNDONGOS ENDOGAMICOS BALB C
MYCOBACTERIUM LEPRAE
MYCOBACTERIUM LEPRAE
PEROXIDASE
 PEROXIDASES
 PEROXIDASES
 REAÇAO EM CADEIA POR POLIMERASE
 DNA POLIMERASE DIRIGIDO POR RNA
 CONTAGEM DE CINTILAÇAO
 HOMOLOGIA DE SEQUENCIA DO ACIDO NUCLÉICO
 ESPECTROFOTOMETRIA
Location:BR191.1; 08638/s



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