Flavobacterium Heparinum
Mostrando 1-12 de 19 artigos, teses e dissertações.
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1. Heparinases: Clonagem, Expressão e Requisitos Estruturais para a Atividade. / Heparinases: Cloning, Expression and Structural Requirements for Activity.
Características estruturais de heparina (Hep) e heparam sulfato (HS) têm sido determinadas usando enzima de Flavobacterium heparinum, uma bactéria de solo, não-patogênica. Sob indução com Hep/HS ou seus dissacarídeos como única fonte de carbono e nitrogênio, a bactéria sintetiza heparinase e heparitinases I e II. Essas liases clivam heparina e HS
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 27/04/2011
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2. Caracterização molecular da enzima heparinase II de flavobacterium heparinum através de simulações de dinâmica molecular
A hemostasia envolve diversos eventos fisiológicos desencadeados após a ruptura da integridade vascular. Durante estes processos, os glicosaminoglicanos, incluindo a heparina e o heparan sulfato, desempenham funções fisiológicas fundamentais. Particularmente a heparina, isolada no início do século XX, permanece até os dias atuais como um dos mais efi
Publicado em: 2009
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3. Sulfur regulation of heparinase and sulfatases in Flavobacterium heparinum.
Sulfur regulation of heparinase synthesis and sulfatase synthesis was studied in Flavobacterium heparinum. Heparinase synthesis was strongly repressed by sulfate and L-cysteine, while the activity of this enzyme showed little or no inhibition by these compounds. Heparinase was synthesized in the absence of heparin when L-methionine was used as the sole sulfu
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4. Expression System for High Levels of GAG Lyase Gene Expression and Study of the hepA Upstream Region in Flavobacterium heparinum
A system for high-level expression of heparinase I, heparinase II, heparinase III, chondroitinase AC, and chondroitinase B in Flavobacterium heparinum is described. hepA, along with its regulatory region, as well as hepB, hepC, cslA, and cslB, cloned downstream of the hepA regulatory region, was integrated in the chromosome to yield stable transconjugant str
American Society for Microbiology.
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5. Isolation and Expression in Escherichia coli of cslA and cslB, Genes Coding for the Chondroitin Sulfate-Degrading Enzymes Chondroitinase AC and Chondroitinase B, Respectively, from Flavobacterium heparinum
In medium supplemented with chondroitin sulfate, Flavobacterium heparinum synthesizes and exports two chondroitinases, chondroitinase AC (chondroitin AC lyase; EC 4.2.2.5) and chondroitinase B (chondroitin B lyase; no EC number), into its periplasmic space. Chondroitinase AC preferentially depolymerizes chondroitin sulfates A and C, whereas chondroitinase B
American Society for Microbiology.
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6. Cloning and expression of heparinase I gene from Flavobacterium heparinum.
Heparinases, enzymes that cleave heparin and heparin sulfate, are implicated in physiological and pathological functions ranging from wound healing to tumor metastasis and are useful in deheparinization therapies. We report the cloning of the heparinase I (EC 4.2.2.7) gene from Flavobacterium heparinum using PCR. Two degenerate oligonucleotides, based on the
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7. Heparinase production by Flavobacterium heparinum.
Heparinase production by Flavobacterium heparinum in complex protein digest medium, with heparin employed as the inducer, has been studied and improved. The maximum productivity of heparinase has been increased 156-fold over that achieved by previously published methods to 375 U/liter per h in the complex medium. Rapid deactivation of heparinase activity, bo
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8. Specific plate assay for bacterial heparinase.
A procedure was developed for detecting heparinase activity on heparin agar plates. The method is based on the differential precipitation of heparin and heparinase-generated heparin fragments by protamine sulfate. Heparinase activity is detected by the presence of clear zones against a white background. This method can be used to screen for the expression of
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9. Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum.
Upon induction with heparin, Flavobacterium heparinum synthesizes and secretes into its periplasmic space heparinase I (EC 4.2.2.7), heparinase II, and heparinase III (heparitinase; EC 4.2.2.8). Heparinase I degrades heparin, and heparinase II degrades both heparin and heparan sulfate, while heparinase III degrades heparan sulfate predominantly. We isolated
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10. Purification and properties of Bacteroides heparinolyticus heparinase (heparin lyase, EC 4.2.2.7).
Heparinase (heparin lyase, EC 4.2.2.7) was isolated from the cell extract of an oral bacterium, Bacteroides heparinolyticus. It was a basic protein with an isoelectric point of 9.5. Its molecular weight was 63,000. The enzyme was the most active against heparin among the tested mucopolysaccharides. Catalytic properties may be similar to those of heparinase o
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11. Natural relationship between bacteroides and flavobacteria.
Comparisons among 16S rRNA sequences from various eubacteria reveal a natural relationship between the bacteroides (represented by the Bacteroides fragilis sequence) and a phylogenetic unit that comprises the flavobacteria, cytophagae, flexibacteria, and others (represented by the Flavobacterium heparinum sequence). Although the relationship is not a close o
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12. Chondroitinase-Producing Bacteria in Natural Habitats
A search was undertaken for bacteria which degrade chondroitin sulfate in nature and to find bacteria with a usefully high rate of chondroitinase (ChSase) productivity. First, 253 ChSase-producing bacteria were obtained from aquatic and land environments in Japan by aerobic and anaerobic screening methods. Identification according to Bergey's Manual of Deter