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Competitive Adsorption of Albumin and Fibrinogen at Solution—Air and Solution—Polyethylene Interfaces

1995; American Chemical Society; Linguagem: Inglês

10.1021/bk-1995-0602.ch015

1947-5918

Adam Baszkin, Marie Martine Boissonnade,

Blood properties and coagulation

The in situ adsorption measuring procedure based on the use of 14C (β-emitting radiation) labeled proteins has been developed in our laboratory in the early 80s. The main advantage of this procedure over other methods in which (γ-emitting radiation) labeled proteins are used for adsorption studies is that no rinsing of samples is necessary to detect the surface protein concentration. We have then extended this method to sequential and competitive protein adsorption studies at the interfaces with polymers. The adsorption of albumin and fibrinogen was studied at solution-air and solution-polyethylene interfaces. The results show that while on both studied interfaces albumin adsorption was insensitive to the pH variation, fibrinogen exhibited a strong enhancement in adsorption in the neighbourhood of its isoelectric point (IEP). The reversibility of adsorption at the polyethylene interface occured both for albumin and fibrinogen in a wide range of pHs but the effect was more pronounced for the latter. Competitive adsorption experiments at the solution-air interface reveal that albumin was not capable of substantially reduce fibrinogen adsorption and that this tendency decreased when albumin solution concentration increased. Conversely, on polyethylene at sufficiently high solution concentrations, fibrinogen adsorption was higher than its adsorption from the single protein system.