A simple centrifugation technique has been developed to study the interaction of human coagulation Factors IXa and X with phospholipid membranes. In the presence of Ca2+, equimolar phosphatidylserine/phosphatidylcholine membranes form tight complexes with Factor X (KD = 2.8 × 10(-8) M); the KD is independent of the phospholipid concentration. Binding sites are available for about 2 mmol of Factor X/mol of phospholipid. Factor IXa has a slightly higher affinity for the phospholipid membrane (KD = 1.2 × 10(-8)M), and competes with Factor X for binding. The experimentally observed competition between Factor X and Factor IXa is in agreement with a model that describes the binding of two distinct ligands to a single class of independent binding sites.
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November 1984
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Research Article|
November 01 1984
Binding of human blood-coagulation Factors IXa and X to phospholipid membranes
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1984 London: The Biochemical Society
1984
Biochem J (1984) 223 (3): 599–605.
Citation
K Mertens, R Cupers, A Van Wijngaarden, R M Bertina; Binding of human blood-coagulation Factors IXa and X to phospholipid membranes. Biochem J 1 November 1984; 223 (3): 599–605. doi: https://doi.org/10.1042/bj2230599
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