Voprosy meditsinskoi khimii (ISSN 0042-8809)

Influence of lectin glycine max to protrombin interaction with erythrocytes

Zubairov D.M., Kiselev S.V., Bulatova A.I.
PubMed Id: 9312937
Year: 1997 vol: 43  issue:4  pages: 226-232
Abstract: Native porcine erythrocytes do not initiate blood coagulation, though even the weak association (Kd = 4,25 +/- 9,35 microM) of prothrombin with their surface which is limited to the projection of two phospholipid polar head groups onto the external cell membrane, exerts a slight but authentic influence on the acceleration of blood clotting. There are 11.9 x 10(7) sites for 125I-prothrombin on one erythrocytes. At physiological concentration of prothrombin the surface of erythrocytes is far from saturation. The binding of 125I-labelled prothrombin to erythrocytes after their surface was covered by lectin Glycine max by means of the accessible residues of N-acetyl-D-galactosamine and D-galactose, glycoproteins and dlycolipids can never become saturated with any used concentration of the ligand. In the presence of the suspension of erythrocytes treated lectin platelet free plasma coagulates at the same speed as the control plasma.
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Reference: Zubairov D.M., Kiselev S.V., Bulatova A.I., Influence of lectin glycine max to protrombin interaction with erythrocytes, Voprosy meditsinskoi khimii, 1997, vol: 43(4), 226-232.