Properties and regional distribution of cerebral CMP-N-acetylneuraminic acid: Glycoprotein sialyltransferase |
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Authors: | Dick H Van Den Eijnden Willem Van Dijk |
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Institution: | Department of Chemical Physiology, Vrije Universiteit, Van der Boechorststraat 7- P.O. Box 7161, Amsterdam, The Netherlands |
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Abstract: | Glycoprotein sialyltransferase was studied in the rat brain and in the frontal grey cortex and corpus callosum of the calf brain. Activities were measured with endogenous acceptors as well as with desialized α1-acid glycoprotein as an exogenous acceptor. The enzyme was characterized by means of its pH optimum, Km values and requirements for detergent and cations. The properties of the rat and calf brain enzymes appeared to be very similar. Substrate specificity studies indicate that more than one glycoprotein sialyltransferase reaction may occur in brain. The regional distribution of the enzyme in the calf brain was rather uniform. From this it was concluded that glycoprotein sialyltransferase, at least for the greater part, is localized in membranes other than those of the synaptic complexes, and occurs in both neurons and glia cells. The regional distribution of the amounts of endogenous glycoprotein acceptor sites, which could be calculated from the sialyltransferase activities, showed a striking correlation with that of the protein-bound sialic acid, but not with the sialyltransferase activity. The role of these endogenous glycoprotein acceptors in cerebral sialoglycoprotein biosynthesis is discussed. |
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Keywords: | CMP-AcNeu GlcNAc GalNAc Man mannose Gal galactose |
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