Muramidase
Mostrando 1-12 de 83 artigos, teses e dissertações.
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1. Variable related to the Trypanosoma cruzi (Chagas, 1909) and to the Triatoma brasiliensis vector (Neiva, 1911) that intervenes in the host-parasite relations / Variáveis relacionadas ao Trypanosoma cruzi (Chagas, 1909) e ao vetor Triatoma brasiliensis (Neiva, 1911) que interferem na interação parasito-hospedeiro
Despite of the multiclonal structure and genetical variability of Trypanosoma cruzi (Chagas, 1909), several investigations using the eletrophoretic profiles (zymodeme) and molecular techniques were used to characterize subpopulations of this parasite, further defining two main distinct and distant phylogenetic lineages: T. cruzi (TcI and TcII). In the presen
Publicado em: 2006
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2. Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790.
A substantial portion of the second peptidoglycan hydrolase (muramidase-2) activity of Enterococcus hirae ATCC 9790 (formerly Streptococcus faecium) is present in the supernatant culture medium. In contrast, nearly all muramidase-1 activity is associated with cells in the latent, proteinase-activatable form. Muramidase-2 activity is produced and secreted thr
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3. Identification of a gene (arpU) controlling muramidase-2 export in Enterococcus hirae.
Muramidase-2 of Enterococcus hirae is a 74-kDa peptidoglycan hydrolase that plays a role in cell wall growth and division. To study its regulation, we isolated a mutant defective in muramidase-2 release under certain growth conditions. This mutant had cell walls which apparently lacked 74-kDa muramidase-2 but which accumulated two proteolytic fragments of 32
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4. Bactericidal activity of human lysozyme, muramidase-inactive lysozyme, and cationic polypeptides against Streptococcus sanguis and Streptococcus faecalis: inhibition by chitin oligosaccharides.
The basis of the bactericidal activity of human lysozyme against Streptococcus sanguis was studied. Experiments were designed to evaluate the role of lysozyme muramidase activity in its bactericidal potency. Inactivation of the muramidase activity of lysozyme was achieved by reduction of essential disulfides with dithiothreitol (DTT) or by incubation with th
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5. Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC 824 that acts on non-N-acetylated peptidoglycan.
An extracellular enzyme showing lytic activity on non-N-acetylated peptidoglycan has been isolated from Clostridium acetobutylicum ATCC 824. The lytic enzyme was purified to homogeneity by anion-exchange chromatography and gel filtration, with a recovery of 24%. The enzyme was monomeric and had an estimated molecular weight of 41,000 and an isoelectric point
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6. The distribution of muramidase (lysozyme) in human tissues.
The distribution of muramidase (lysozyme) in normal and pathological human tissues has been studied, using an immunohistological technique. The enzyme was demonstrated in a variety of healthy tissues, including serous salivary acinar cells, lactating mammary tissue, Paneth cells, renal tubular cells, myeloid cells (including eosinophils), and histiocytic cel
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7. Structures Suggesting Cell-Wall-Deficient Forms Detected in Circulating Erythrocytes by Fluorochrome Staining
Cell-wall-deficient (CWD) forms of bacteria are associated with certain cases of idiopathic septicemia. In this preliminary study of blood examined immediately after venipuncture, structures with a morphology characteristic of CWD forms were seen parasitizing the erythrocytes. These inclusions were usually circumferential, but in some cases they protruded fr
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8. Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene.
The exudate of fully germinated spores of Clostridium perfringens S40 in 0.15 M KCI-50 mM potassium phosphate (pH 7.0) was found to contain another spore-lytic enzyme in addition to the germination-specific amidase previously characterized (S. Miyata, R. Moriyama, N. Miyahara, and S. Makino, Microbiology 141:2643-2650, 1995). The lytic enzyme was purified to
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9. The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin.
A second peptidoglycan hydrolase (muramidase-2) of Streptococcus faecium ATCC 9790 (Enterococcus hirae) has been purified to apparent homogeneity. The enzyme has been shown to be a beta-1,4-N-acetylmuramoylhydrolase (muramidase; EC 3.2.1.17) and to differ in substrate specificity from a previously isolated muramidase. Purified enzyme appears as two protein s
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10. Ultrastructural localisation of muramidase in the human synovial membrane.
The synovial intimal cell layer comprises two morphological types of cell, A and B, with an intermediate type also postulated. Type A cells show features in common with other cells of the mononuclear phagocyte system, while type B cells appear similar to fibroblasts and are assumed to have synthetic activity. Muramidase is a marker of mononuclear phagocytic
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11. Penicillin tolerance in Streptococcus faecium ATCC 9790.
Tolerant strains of Streptococcus faecium had higher levels of muramidase 2 and lower levels of trypsinactivable muramidase 1 than did susceptible strains. Susceptible strains lysed faster than did tolerant strains in buffer and at some antibiotic concentrations. The addition of Triton X-100 produced equal lysis rates for susceptible and tolerant cultures.
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12. Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali.
DD-Carboxypeptidase (DD-CPase) activity of Enterococcus hirae (Streptococcus faecium) ATCC 9790 was extracted from intact bacteria and from the insoluble residue (crude cell wall fraction) of mechanically disrupted bacteria by a brief treatment at pH 10.0 (10 mM glycine-NaOH) at 0 degrees C or by extraction with any of several detergents. Extractions with hi