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N-DSK gamma-chain binds to immunoprecipitated GP IIb-IIIa

Journal Article · · Thromb. Res.; (United States)

The CNBr-split N-terminal disulphide knot of the fibrinogen molecule (N-DSK) binds to ADP-stimulated gel-filtered platelets and immunoprecipitated fibrinogen receptor. To investigate which part of the N-DSK molecule that is involved in this binding, the glycoprotein IIb-IIIa complex (the fibrinogen receptor) was immunoprecipitated in crossed immunoelectrophoresis of Triton X-100 extracts of platelets against rabbit antibodies to whole platelet proteins. The immunoelectrophoresis plates were incubated with solubilized, carboxymethylated /sup 125/I-labelled A alpha -, B beta - or gamma-chains of N-DSK, and investigated for binding by autoradiography. The N-DSK gamma-chain, but not the A alpha - or B beta -chains demonstrated binding to the GP IIb-IIIa complex. These results show that the fibrinogen molecule contains a third sequence of amino acids, in addition to the two previously reported ones that can be involved in binding of fibrinogen to the fibrinogen receptor on the platelets.

Research Organization:
Research Institute for Internal Medicine, Oslo, Norway
OSTI ID:
6030612
Journal Information:
Thromb. Res.; (United States), Journal Name: Thromb. Res.; (United States) Vol. 47:3; ISSN THBRA
Country of Publication:
United States
Language:
English