Russian Journal

ISSN 0042-8809

Issue:
Volume 43, issue 4

Title:
INFLUENCE OF LECTIN GLYCINE MAX TO INTERACTION PROTHROMBIN WITH ERYTHROCYTES

Authors:
D.M.Zubairov, S.V.Kiselev, A.I.Bulatova

Address:
Department of Biochemistry of Kazan state medical university, 420012 Kazan, Butlerov str., 49;
Fax: 007 (8-432) 36-03-93,
electronic post (mail): Dilja@ant.ksc.iasnet.com

Abstract:
Native porcine erithrocytes do not initiate blood coagulation, though even the weak association (Kd=4,25 ñ 0,35 æM) 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 107 sites for 125I-prothrombin on the erythrocyte. At physioligical 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 glycolipids 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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