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  Vol. 246 No. 20, November 20, 1981 TABLE OF CONTENTS
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Hepatic Recognition and Catabolism of Serum Glycoproteins

Gilbert Ashwell, MD; Clifford J. Steer, MD

JAMA. 1981;246(20):2358-2364.

Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

WITH THE exception of albumin, essentially all serum proteins are glycoproteins, that is, proteins to which one or more carbohydrate chains are bound in covalent linkage. The sugars most commonly found in association with proteins are galactose, mannose, N-acetylhexosamine, sialic acid, and fucose. Glucose occurs rarely, if at all, as a normal constituent of circulating proteins.

In general, the carbohydrate moiety may be envisaged as consisting of two domains. The outer, nonreducing terminus is composed of the trisaccharide, sialic acid-galactose-N-acetylglucosamine. Usually, between two and four such terminal triads may be linked glycosidically to the second domain, which is composed of three mannose and two N-acetylglucosamine residues. The structure of a typical, complex carbohydrate chain is illustrated in the Figure. On treatment with neuraminidase, the sialic acid moiety is cleaved to reveal the penultimate galactose moiety as the new, nonreducing termini of the resulting asialoglycoprotein. Fucose, which . . . [Full Text PDF of this Article]


Author Affiliations

From the Laboratory of Biochemistry and Metabolism, National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Md.


Footnotes

Reprint requests to National Institutes of Health, Department of Health and Human Services, Bldg 10, Room 9N-105, Bethesda, MD 20205 (Dr Ashwell).



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