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- W1849674759 abstract "Dans le cerveau, I'activité mannosyl-transférase, du GDP-mannose à un accepteur glycoprotéinique endogène, est localisée au niveau de la fraction des microsomes et fragments de synaptosomes des cellules cérébrales. Ce système polyenzymatique complexe se caractérise par deux maxima d'activitéà deux pH différents, respectivement 5,9 et 7,4. Le système est activé après une pré-incubation à température supra-optimale, qui modifie les conditions d'environnement enzyme-substrat. I1 est également activé par le Triton X-100 à certaines concentrations, et par les cations Mn2+ et Mg2+. A I'opposé, il est inhibé par les nucleosides-diphosphates, le GTP et le β-γ-methylène-GTP. Le cycloheximide n'a pas d'effet sur la transglycosylation, mais la puromycine réduit I'activité mannosyl-transférase. Ceci met en évidence I'importance, dans le modèle cérébral, de la persistance de l'attachement des chaines polypeptidiques aux polysomes pendant I'exécution du processus de transglycosylation. In the brain, mannosyl-transferase activity, from GDP-mannose to glycoproteins, is localized in a subcellular fraction including microsomes and synaptosome fragments. This enzymic complex has two maxima of activity, at pH 5·9 and 7·4. It is activated by pre-incubation at supraoptimal temperatures which modifies the enzyme-substrate environment, and is activated also by the detergent Triton X-100 and by the cations Mn2+ and Mg2+, but is inhibited by nucleoside-diphosphates, GTP and βγ-methylene GTP. Cycloheximide has no effect on transglycosylation, but puromycin reduces the mannosyl-transferase activity. This is interpreted as good evidence for the importance of attachment of the polypeptide chain to polysomes during transglycosylation." @default.
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- W1849674759 date "1971-12-01" @default.
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- W1849674759 title "BIOSYNTHESE DES GLYCOPROTEINES CEREBRALES: ETUDE DE L'ACTIVITE MANNOSYL-TRANSFERASE PARTICULEE DU CERVEAU." @default.
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- W1849674759 doi "https://doi.org/10.1111/j.1471-4159.1971.tb00185.x" @default.
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