D N Acetylglucosaminidase
Mostrando 1-12 de 41 artigos, teses e dissertações.
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1. Atividade β-D-N-Acetilglucosaminidásica de enzimas imobilizadas extraídas da Artemia franciscana e possíveis aplicações biotecnológicas
A β-D-N-acetilglucosaminidase, extraída e parcialmente isolada do crustáceo Artemia franciscana através de precipitação com sulfato de amônio e cromatografia em gel filtração Bio Gel A 1.5m foi imobilizada em Dacron ferromagnético rendendo um derivado insolúvel ativo contendo 5,0 unid/mg de proteína e retendo 10,35% da atividade da enzima sol
Publicado em: 2008
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2. Increase in β-N-Acetylglucosaminidase Activity during Germination of Cotton Seeds 1
A marked increase in β-acetylglucosaminidase (2-acetamido-2-deoxy-β-d-glucoside acetamidodeoxyglucohydrolase, EC 3.2.1.30) activity was observed in the germinating cotyledon of cotton seeds. The enzyme was isolated from cotton seedlings and purified to study its physiological function in the germination of cotton seeds. The purification procedure involves
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3. Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli.
beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophenyl-beta-D-2-acetamido-2-deoxyglucopyranoside is 0.43 mM. The molecular we
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4. Chitin-binding hemagglutinin produced by Conidiobolus strains.
A hemagglutinin was produced by strains of Conidiobolus which also produce beta-N-acetylglucosaminidase. Activity of the hemagglutinin was inhibited by D-glucosamine, N-acetyl-D-glucosamine, D-mannosamine, and beta-N-acetyl-D-glucosaminides but not by D-glucose, D-mannose, and alpha-N-acetyl-D-glucosaminides.
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5. Molecular cloning and expression of the Candida albicans beta-N-acetylglucosaminidase (HEX1) gene.
beta-N-Acetylglucosaminidase was purified from the spent culture medium of Candida albicans A72 grown in the presence of N-acetylglucosamine (GlcNAc). The N-terminal amino acid sequence of the protein was determined, two degenerate oligonucleotide probes were constructed, and a 3.9-kb BamHI fragment of DNA that hybridized to both probes was subcloned from a
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6. Purification of glycoside hydrolases from Bacteroides fragilis.
Six glycoside hydrolases in the culture medium of Bacteroides fragilis--alpha-glucosidase, beta-glucosidase, alpha-galactosidase, beta-galactosidase, beta-N-acetylglucosaminidase, and alpha-L-fucosidase-were systematically purified by ammonium sulfate precipitation, gel filtration chromatography, and density gradient isoelectric focusing. The isoelectric foc
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7. Mucin Degradation in Human Colon Ecosystems: EVIDENCE FOR THE EXISTENCE AND ROLE OF BACTERIAL SUBPOPULATIONS PRODUCING GLYCOSIDASES AS EXTRACELLULAR ENZYMES
Recent work indicates that subpopulations of human fecal bacteria, averaging ∼1% of the total viable fecal flora, degrade the oligosaccharide side chains of hog gastric mucin, which structurally resembles human epithelial mucins. Here we report studies to determine whether degradation of mucin oligosaccharides is related to glycosidase production by bacter
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8. Primate cytomegalovirus glycoproteins: lectin-binding properties and sensitivities to glycosidases.
The lectin-binding properties and glycosidase sensitivities of the virion glycoproteins of primate cytomegaloviruses (CMVs) were examined. Three simian CMV (SCMV) strains, including Colburn, and four human CMV (HCMV) strains were compared. Their proteins were separated in denaturing polyacrylamide gels and electrotransferred onto nitrocellulose, and the glyc
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9. Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis: Identification of a Third N-Acetylglucosaminidase, AcmC
The peptidoglycan hydrolase (PGH) complement of Lactococcus lactis was identified by amino acid sequence similarity searching of the L. lactis IL-1403 complete genome sequence. Five PGHs that are not encoded by prophages were detected, including the previously characterized AcmA and AcmB proteins. Four of these PGHs, AcmA to AcmD, contain a catalytic domain
American Society for Microbiology.
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10. Biogenesis of membrane-bound and secreted immunoglobulins: two primary translation products of the human delta chain, differentially N-glycosylated to four discrete forms in vivo and in vitro.
Structural differences between the heavy chain of membrane IgD (delta m) and the heavy chain of secreted IgD (delta s) were investigated by using a human lymphoblastoid cell line that expresses idiotypically identical IgM and IgD. In a wheat germ cell-free system, mRNA from this cell line was shown to encode two distinct delta chains that differed in molecul
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11. Mode of action of pesticin: N-acetylglucosaminidase activity.
Homogeneous preparations of pesticin, a bacteriocin produced by Yersinia pestis, neither significantly inhibited net synthesis of deoxyribonucleic acid, ribonucleic acid, or protein in Escherichia coli phi nor caused detectable degradation of deoxyribonucleic acid in vivo. Accordingly, its mode of action does not resemble that of colicin E2 as suggested by o
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12. Sucrose Synthase, a Cytosolic Enzyme in Protoplasts of Jerusalem Artichoke Tubers (Helianthus tuberosus L.) 1
The exact subcellular location of sucrose synthase (UDP-d-glucose: d-fructose 2-α-d-glucosyltransferase, EC 2.4.1.13) in Helianthus tuberosus tubers was studied by comparison of its activity in protoplasts with that of vacuoles isolated from them. Assuming 100% of the β-N-acetylglucosaminidase activity to be of vacuolar origin, less than 5% of both the suc