Aspartic Proteinases
Mostrando 1-12 de 24 artigos, teses e dissertações.
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1. Caracterização de proteinases envolvidas na geração de peptídeos antimicrobianos no intestino de Rhipicephalus (Boophilus) microplus. / CE. Characterization of proteinases involved in the generation of antimicrobial peptides in the gut of Rhipicephalus (Boophilus) microplus.
It is known that hemoglobin is a rich source of antimicrobial peptides (hemocidins). The first hemoglobin-derived hemocidin characterized in ticks was the peptide Hb33-61, which is active against Gram-positive bacteria and fungi. It is believed that hemocidins are endogenously generated in the tick gut. In this work we biochemically characterized a cathepsin
Publicado em: 2010
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2. Anti-oxidative and proteolytic activities and protein profile of laticifer cells of Cryptostegia grandiflora, Plumeria rubra and Euphorbia tirucalli
In this study, proteins extracted from laticifer cells of three plants were examined by electrophoresis, mass spectrometry (MALDI-TOF) and characterized in respect of proteolytic, chitinolytic and anti-oxidative activities by means of zymography and colorimetric assays. Acidic proteins with molecular masses between 12.5 and 74.5 kDa predominated in laticifer
Brazilian Journal of Plant Physiology. Publicado em: 2010
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3. Isolamento e caracterização de um novo conjunto de serinoproteases com atividade trombina-like e de L-aminoacido oxidase do veneno de Crotalus durissus cascavella / Isolation and characterization of a new serine proteases group with thrombinin-like and L-amino acid oxidase activity from Crotalus durissus cascavella
The use of the isolated toxins from poisons as molecular tools in the understanding of diverse physiological and pathological events has been proved by some works in literature. The serpent Crotalus durissus cascavella is found in the areas of Caatinga Northeast of Brazil, since Maranhão until North of the state of Minas Gerais, and in spite of it hasn?t be
Publicado em: 2006
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4. Ocorrencia de Candida albicans e Candida dubliniensis em sitios subgengivais e nas mucosas da cavidade bucal : genotipagem por RAPD e atividade enzimatica de aspartil proteinases e fosfolipases / Occurrence of Candida albicans and Candida dubliniensis in the subgingival sites and on the mucosa of the oral cavity: genotyping by RAPD and enzimatic activies of aspartic proteinases and phospholipases
Candida spp. são leveduras oportunistas, que habitam a cavidade bucal de uma proporção significativa da população saudável. Entretanto, sob condições predisponentes, podem provocar candidose bucal. Foram avaliados 53 pacientes com diagnóstico de periodontite, porém saudáveis sistemicamente, com o objetivo de verificar a ocorrência destes microrga
Publicado em: 2005
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5. Proteinase activity regulation by glycosaminoglycans
There are few reports concerning the biological role and the mechanisms of interaction between proteinases and carbohydrates other than those involved in clotting. It has been shown that the interplay of enzymes and glycosaminoglycans is able to modulate the activity of different proteases and also to affect their structures. From the large number of proteas
Brazilian Journal of Medical and Biological Research. Publicado em: 2002-02
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6. Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lung.
Hydrolysis of structural proteins in the lung by extracellular proteinases secreted by Aspergillus fumigatus is thought to play a significant role in invasive aspergillosis. This fungus was found previously to secrete an elastinolytic serine proteinase and a metalloproteinase. We report that A. fumigatus also secretes an aspartic proteinase (aspergillopepsin
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7. Retrovirus protease characterized as a dimeric aspartic proteinase.
Retroviruses and retroviruslike elements have a protease for specific cleavage of their polyprotein precursors. On the basis of amino acid sequences conserved among species and the sensitivity to protease inhibitors, it was proposed that the retrovirus protease could be classified as an aspartic proteinase. Since the virus protease molecule is comparable to
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8. Mutational analysis of human immunodeficiency virus type 1 protease suggests functional homology with aspartic proteinases.
Processing of the retroviral gag and pol gene products is mediated by a viral protease. Bacterial expression systems have been developed which permit genetic analysis of the human immunodeficiency virus type 1 protease as measured by cleavage of the pol protein precursor. Deletion analysis of the pol reading frame locates the sequences required to encode a p
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9. Aspartic proteinases: Fourier transform infrared spectroscopic studies of a model of the active side.
We synthesized and studied by Fourier transform infrared spectroscopy nine monosalts of diamides as models for the active side of aspartic proteinases. One compound, the monosalt of meta-aminobenzoic acid diamide of fumaric acid (m-FUM), shows the same biological activity as pepsin with regard to the splitting of peptide bonds of the Pro-Thi-Glu-Phe-Phe(4-NO
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10. Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity.
Enzymatically active retroviral proteinases are dimers of identical polypeptide chains with a fold similar to that of other aspartic proteinases. Each polypeptide chain, encoded on one of the viral polyproteins, is less than half the size of cellular aspartic proteinases and contains only one of the two active-site aspartate residues. A plasmid was construct
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11. Endosomal aspartic proteinases are required for invariant-chain processing.
Immunogenic peptides are displayed in the context of class II histocompatibility proteins on the surface of antigen-presenting cells. Class II alpha and beta subunits bind the invariant chain (I-chain), a transmembrane glycoprotein which must dissociate prior to peptide presentation. Proteolytic release of I-chain in an acidic compartment is followed by clas
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12. Production, Characterization, and Epitope Mapping of a Monoclonal Antibody against Aspartic Proteinase of Candida albicans
A monoclonal antibody (MAb; MAb CAP1) that was reactive with extracellular aspartic proteinase of Candida albicans (CAP) was produced. The MAb showed strong sensitivity and reactivity to CAP but not to the aspartic proteinases of Candida parapsilosis, Candida tropicalis, and Aspergillus fumigatus or to human cathepsin D or porcine pepsin. The epitope o
American Society for Microbiology.