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Literature DB >> 5263019

Biosynthesis of the chondroitin sulfate-protein linkage region: purification and properties of a glucuronosyltransferase from embryonic chick brain.

Abstract

The present paper describes the purification and properties of a glucuronosyltransferase isolated from 13-day embryonic chick brain. The enzyme catalyzes transfer of glucuronic acid from UDP-glucuronic acid to a series of low and high molecular weight compounds which contain terminal non-reducing beta-D-galactose residues. Studies utilizing enzymatically degraded chondromucoprotein as acceptor suggest that the glucuronosyltransferase terminates biosynthesis of the linkage region between protein and polysaccharide of chondromucoprotein.

Entities: Chemical Species

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Year: 1969 PMID： 5263019 PMCID： PMC286172 DOI： 10.1073/pnas.64.1.374

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

24 in total

1. Subcellular co-localization and potential interaction of glucuronosyltransferases with nascent proteochondroitin sulphate at Golgi sites of chondroitin synthesis.

Authors: G Sugumaran; M Katsman; J E Silbert
Journal: Biochem J Date: 1998-01-01 Impact factor: 3.857

1 in total

Biosynthesis of the chondroitin sulfate-protein linkage region: purification and properties of a glucuronosyltransferase from embryonic chick brain.

1. THE BIOSYNTHESIS OF CHONDROITIN SULFATE BY A CELL-FREE PREPARATION.

2. Fractionation of the degradation products of compounds of protein and polysaccharide from cartilage.

3. Isolation of acid mucopolysaccharides of human brain.

4. The sialic acids. VI. Purification and properties of sialidase from Clostridium perfringens.

5. The chondroitin 4-sulfate-protein linkage.

6. Incorporation of D-galactose into glycoproteins.

7. Further characterization of the heparin-protein linkage region.

8. The synthesis of O-serine glycosides.

9. The biosynthesis of chondroitin sulfate.

10. Estimation of the molecular weights of proteins by Sephadex gel-filtration.

1. Subcellular co-localization and potential interaction of glucuronosyltransferases with nascent proteochondroitin sulphate at Golgi sites of chondroitin synthesis.