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1.
Carbohydr Res ; 343(16): 2735-9, 2008 Nov 03.
Artigo em Inglês | MEDLINE | ID: mdl-18550037

RESUMO

An efficient separation between fully acetylated thiosialoside methyl esters and fully acetylated Neu5Ac2en methyl esters was accomplished by means of a size-exclusion chromatography (SEC) method. Purity determinations and structural elucidation of the isolated compounds were performed by a combination of elemental analyses and spectroscopic analyses, including IR, (1)H, and (13)C NMR, and mass spectroscopic analyses.


Assuntos
Cromatografia em Gel , Tioaçúcares/isolamento & purificação , Configuração de Carboidratos , Tioaçúcares/química
2.
Bioorg Med Chem Lett ; 17(14): 3826-30, 2007 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-17524642

RESUMO

A conventional synthesis of alpha-thioglycoside of sialic acid as a glycomonomer was accomplished. Radical copolymerization of the glycomonomer with vinyl acetate proceeded smoothly to afford a new class of glycopolymers having thiosialoside residues, in which all protection was removed by a combination of transesterification and saponification to provide a water-soluble thiosialoside cluster. The results of a preliminary study on biological responses against influenza virus neuraminidases using the thiosialoside polymer as a candidate for a neuraminidase inhibitor showed that the glycopolymer has potent inhibitory activity against the neuraminidases.


Assuntos
Inibidores Enzimáticos/farmacologia , Epitopos/farmacologia , Ácido N-Acetilneuramínico/farmacologia , Neuraminidase/antagonistas & inibidores , Orthomyxoviridae/enzimologia , Polímeros/farmacologia , Inibidores Enzimáticos/química , Espectroscopia de Ressonância Magnética , Ácido N-Acetilneuramínico/química , Polímeros/química , Espectrofotometria Infravermelho
3.
Genome Res ; 16(5): 686-91, 2006 May.
Artigo em Inglês | MEDLINE | ID: mdl-16606699

RESUMO

Protein-protein interactions play key roles in protein function and the structural organization of a cell. A thorough description of these interactions should facilitate elucidation of cellular activities, targeted-drug design, and whole cell engineering. A large-scale comprehensive pull-down assay was performed using a His-tagged Escherichia coli ORF clone library. Of 4339 bait proteins tested, partners were found for 2667, including 779 of unknown function. Proteins copurifying with hexahistidine-tagged baits on a Ni2+-NTA column were identified by MALDI-TOF MS (matrix-assisted laser desorption ionization time of flight mass spectrometry). An extended analysis of these interacting networks by bioinformatics and experimentation should provide new insights and novel strategies for E. coli systems biology.


Assuntos
Escherichia coli K12/química , Proteínas de Escherichia coli/metabolismo , Proteoma/análise , Proteínas de Escherichia coli/química , Biblioteca Gênica , Histidina/química , Modelos Biológicos , Fases de Leitura Aberta , Proteômica , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
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