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Binding of fibrinogen to platelet integrin αIIbβ3 in solution as monitored by tracer sedimentation equilibrium by Germán Rivas; Kirsten Tangemann; Allen P. Minton; Jürgen Engel is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Binding of fibrinogen to platelet integrin αIIbβ3 in solution as monitored by tracer sedimentation equilibrium about?

Fibrinogen showed essentially no binding (KD> 1 mM) to platelet aIIb@ integrin in solution in the presence of Triton or octylglucoside above critical micellar concentrations. Under these conditions the integrin was an a$ monomer. After removal of the detergent from the Triton containing buffer (25 mM W i C I ; , 150 mM NaCI, 1 mM CaCI, 1 m~ MgClz, pH 7.4) the integrin formed aggregates with hemmers 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 p ~) . This value is 10to 100-fold higher than values determined by solid phase assays or with integrins reconstituted onto lipid bilayers.

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Author

Germán Rivas; Kirsten Tangemann; Allen P. Minton; Jürgen Engel

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0952-3499)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)