Platelet activation is accompanied by the appearance on the platelet surface of
approximately 45,000 receptor sites for fibrinogen. The binding of fibrinogen to these …

Several lines of evidence indicate that the platelet membrane glycoprotein IIb-IIIa complex
(GP IIb-IIIa) is necessary for the expression of platelet fibrinogen receptors. The purpose of …

Platelet aggregation requires the binding of fibrinogen to its receptor, a heterodimer
consisting of the plasma-membrane glycoproteins (GP) IIb and IIIa. Although the GPIIb-IIIa …

Platelet membrane glycoprotein IIb-IIIa exists as a calcium-dependent complex of two large
peptides (designated IIb and IIIa) in Triton X-100 solutions, but it remains unknown if these …

Considerable evidence indicates that the glycoprotein (GP) IIb/IIIa complex on human
platelets functions as a receptor for fibrinogen, but little is known about the mechanism of …

The platelet membrane glycoprotein IIb-IIIa complex (GPIIb-IIIa) recognizes peptides
containing the amino acid sequence Arg-Gly-Asp, a sequence present at two locations in the …

Platelet membrane glycoproteins IIb and IIIa form a Ca2+-dependent heterodimer complex
that contains binding sites for fibrinogen, von Willebrand factor, and fibronectin following …

Platelet membrane glycoproteins (GP) IIb and IIIa form a Ca2+-dependent, heterodimer
complex (GP IIb-IIIa) in detergent solution. To determine whether these glycoproteins were …

Fibrinogen binding to receptors on stimulated platelets is a prerequisite for platelet
aggregation. To gain further insight into the role of fibrinogen in platelet aggregation and to …

A murine monoclonal antibody, designated AP-2, reacts specifically with the complex formed
by human platelet membrane glycoproteins IIb and IIIa, but does not react at all with the …