Work

Studies on the Chemical and Enzymatic Modification of Glycoproteins

Year: 1971

Type: article

Abstract: A general method is described for the radioactive labeling of proteins containing terminal sialic acid in the carbohydrate moieties. Quantitative conversion of these residues to a radioactive 7-carbon analogue of sialic acid was achieved by sequential periodate oxidation and tritiated borohydride reduction. Evidence is presented to establish the identity of the radioactive derivative as 5-acetamido-3, 5-dideoxy-l-arabino-2-heptulosonic acid and to indicate it as the sole site of tritium incorporation in the carbohydrate chain. Upon injection into rats, labeled preparations of ceruloplasmin and orosomucoid exhibited a normal half-life in the plasma and proved suitable for metabolic studies. The data indicate that the 7-carbon sialic acid analogue mimics sialic acid with respect to hydrolysis by neuraminidase and in regulating survival of glycoproteins in the circulation.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)62392-0

Authors: Lee Van Lenten, Gilbert Ashwell

Institution: National Institutes of Health

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430