Database : HANSEN Search on : PEROXIDASES [Subject descriptor] References found : 3 [refine] Displaying: 1 .. 3   in format [Detailed]

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Id: 13489 Author: Gómez-Estrada, Hector; Morales-Ortiz, Roberto; González-Mendoza, Amado; Barba-Rubio, Jose; Ceja-Mendoza, Sagrario Title: Peroxidase deficiency in histiocytes of patients with nodular lepromatous leprosy ..- Source: s.l; s.n; Apr.-Jun. 1983. 11 p. ilus, tab. Abstract: The purpose of this study was to investigate the presence of peroxidase (PO) in the histiocytes which are found in the lepromatous lesions of patients with nodular lepromatous leprosy (NLL). We studied dermoepidermal biopsy specimens from lepromstous lesions and blood smears of 10 patients with NLL, eight males and twoo females 28 to 63 years age (average 45 + or - 6.2), of which nine coursed with the stable form of the disease and one was in lepromatous reaction. Six had received treatment with diaminodiphenylsulphone for more than six months, and the other four, none. As controls we studied the blood smears of 10 healthy controls and 10 rat liver sections. PO was investigated in histiocytes, Kupffer cells and polymorphonuclears by dichlorhydrate oxydation, according to the technique of Kaplow. By means of Fite-Faraco´s stain, all ten cases proved to have abundant phagocytized M. leprae. PO was not found in histiocytes of lepromatous lesions in nine cases of stable NLL in lepromatous reaction. PO was present in Kupffer cells, in polymorphonuclears of patients with NLL and in controls. No difference was found either in the PO or M. leprae contents between treated and untreated patients. The PO deficiency in histiocytes of patients with NLL may be related to an incapacity of these cells to destroy M. leprae.(AU). Descriptors: PELE/enzimol PELE/patol FAGOCITOSE PEROXIDASES/defic HANSENIASE/enzimol HANSENIASE/patol HISTIOCITOS/enzimol Limits: HUMANO ANIMAL MASCULINO FEMININO ADULTO MEIA-IDADE IDOSO RATOS Electronic Medium: http://www.ilsl.br Location: BR191.1; 01309/s

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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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