Glycopeptides from Bovine Aorta Glycoprotein
Year: 1966
Type: article
Abstract: Studies of glycoprotein material from bovine aorta, purified by gel electrophoresis, indicated the presence of two glycopeptide units. The two glycopeptides were isolated after digestion of the glycoprotein with Pronase after removal of sialic acid by mild acid hydrolysis. The glycopeptides were separated by chromatography on columns of Dowex 50W-X2 (H+) and cellulose. One of the glycopeptides occurred in a concentration approximately 3 times greater than the other. Analysis of the NH2 and COOH end groups and studies by repeated Edman degradation of the major glycopeptide indicated the sequence, -Ala-Phe-Gly-Asp-Gly-. The carbohydrate unit of this glycopeptide consisted of N-acetylglucosamine, galactose, mannose, and fucose. A disaccharide consisting of glucosamine and galactose was obtained by mild acid hydrolysis, and further study indicated this to be 4-O-β-d-galactopyranosyl-d-glucosamine. Periodate oxidation suggested the possibility of branching within the oligosaccharide chain. The glycopeptide unit is similar in many respects to those isolated from glycoproteins from several sources. The other glycopeptide unit which occurred in a lower concentration was unique in that it contained glucose as well as galactose and fucose in the carbohydrate portion. -Gly (Ser, Gly, Phe) Phe- composed the amino acid chain. The site of linkage of the sialic acid to one or both glycopeptides is not known.
Source: Journal of Biological Chemistry
Institution: Louisiana State University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1523701607