Collagen at interfaces. II: Competitive adsorption of collagen against albumin and fibrinogen.
Adsorption of chemically radiolabeled [14C] collagen from binary mixtures with albumin or fibrinogen was studied on the solution/air and solution/polyethylene interfaces and revealed the preferential adsorption of albumin. This phenomenon is confirmed by the data of surface tension measurements of single protein, collagen-albumin, and collagen-fibrinogen solutions. Desorption experiments clearly show that more irreversibly adsorbed collagen was found on polyethylene surfaces when adsorption was performed from collagen-fibrinogen than from collagen-albumin solutions. The combined adsorption-desorption and the surface tension data show that competitive adsorption of collagen at the hydrophobic surfaces is strongly influenced by the surface tension properties of the proteins in solution.
D000327:Adsorption; D000388:Air; D000418:Albumins / Q000378:metabolism*; D000818:Animals; D003094:Collagen / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D011095:Polyethylenes; D051381:Rats; D013499:Surface Properties
D000418:Albumins; D011095:Polyethylenes; D005340:Fibrinogen; D003094:Collagen