Microheterogeneity of Plasma Glycoproteins Antithrombin III and Heparin Cofactor II and Their Carbohydrate Analysis

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Authors
Kim, Yeong Shik
Lee, Kyung Bok
Linhardt, Robert J.
Issue Date
1988-07-01
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Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
Antithrombin III is the most important protease inhibitor in the blood coagulation cascade. Its activity results from the formation of covalent complexes with Factor Xa and thrombin (FIIa) (1). The rate of this inhibition is accelerated up to 2,000-fold in the presence of catalyst, heparin (1). AT111 is a single-chain glycoprotein reportedly containing 9-17% of carbohydrate (2,3). Multiple isoforms of AT111 have been detected by the isoelectric focusing of plasma and purified protein and this microheterogeneity has been attributed to variable sialation (4-7). Recently, a second heparin cofactor has been identified and purified from plasma (8-10). Heparin cofactor II (HCII) is also a glycoprotein, which is antigenically distinct from AT111 and inhibits only FIIa in the presence of heparin (8). Its carbohydrate structure and isoelectric point have not been reported. We confirm the presence of multiple IEF bands for HCII (8). Unlike AT111 it remains heterogeneous even after desialation. Ion-exchange chromatography with pulsed- amperometric detection is used for the first time, on microgram quantities of glycoprotein, to determine the concentration of each neutral sugar, amino sugar and sialic acid residue. The carbohydrate composition of AT111 and HCII are reported.
Description
Thrombosis Research, 51, 97-104
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Full Citation
Microheterogeneity of Plasma Glycoproteins Antithrombin III and Heparin Cofactor II and Their Carbohydrate Analysis, Y.S. Kim, K.B. Lee and R.J. Linhardt, Thrombosis Research, 51, 97-104 (1988).
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493848
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