Work

Binding of Fibrinogen to Platelet Integrin αIIbβ3 in Solution as Monitored by Tracer Sedimentation Equilibrium

Year: 1996

Type: article

Abstract: Fibrinogen showed essentially no binding (KD > 1 mM) to platelet alpha IIb beta 3 integrin in solution in the presence of Triton or octylglucoside above critical micellar concentrations. Under these conditions the integrin was an alpha beta monomer. After removal of the detergent from the Triton containing buffer (25 mM Tris/HCl;, 150 mM NaCl, 1 mM CaCl2, 1 mM MgCl2, pH 7.4) the integrin formed aggregates with hexamers as the most prominent species, as demonstrated by analytical ultracentrifugation and electron microscopy. Tracer sedimentation equilibrium experiments indicate that fibrinogen binds to the integrin aggregates, but with a surprisingly large KD (at least 3 microM). This value is 10- to 100-fold higher than values determined by solid phase assays or with integrins reconstituted onto lipid bilayers.

Source: Journal of Molecular Recognition

DOI: 10.1002/(sici)1099-1352(199601)9:1<31::aid-jmr237>3.0.co;2-o

Authors: Germán Rivas, Kirsten Tangemann, Allen P. Minton, Jürgen Engel

Institutions: University of Basel, National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

Open Access status: bronze

Funders: National Science Foundation, Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

OpenAlex ID: W2009740151

FWCI: 0.451

Cites: 52

Cited by: 11

Related to: 10