Protein absorption and desorption phenomena on clean metal surfaces.
The noncompetitive adsorption of the proteins albumin and fibrinogen onto 17 different metal surfaces has been studied in vitro using 125I-labeled proteins. Although many of the metals showed very similar adsorption characteristics to polymers, several of them adsorbed considerably greater amounts. Copper, gold, and silver were the most significant in this respect, all three being face-centered cubic, group 1B metals known to bind to many types of protein in vitro and in vivo. The desorption of the proteins was studied in an in vivo model in which preproteinized metals were implanted in rats. There was considerable variations in the amounts of the proteins removed from the various metal surfaces. Generally those metals onto which protein is most readily adsorbed tend to lose the protein quickly, whereas others, such as iron, with only moderate adsorbed amounts, may retain a large part of the adsorbed layer for a long time.
D000327:Adsorption; D000818:Animals; D003300:Copper; D005340:Fibrinogen; D006046:Gold; D007457:Iodine Radioisotopes; D008670:Metals; D051381:Rats; D012709:Serum Albumin; D012834:Silver
D007457:Iodine Radioisotopes; D008670:Metals; D012709:Serum Albumin; D012834:Silver; D006046:Gold; D003300:Copper; D005340:Fibrinogen