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. 1984 Nov 1;223(3):599-605.
doi: 10.1042/bj2230599.

Binding of human blood-coagulation Factors IXa and X to phospholipid membranes

K Mertens, R Cupers, A Van Wijngaarden, R M Bertina

Binding of human blood-coagulation Factors IXa and X to phospholipid membranes

K Mertens et al. Biochem J. .

Abstract

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 X 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 X 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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