Interaction of plasma proteins with artificial surfaces: protein adsorption isotherms.
A simple technique using a small disc which is dipped into a 125I-labeled protein solution has been devised to study the adsorption of human albumin, fibrinogen, and IgG onto Cuprophane or PVC. The purity of these human plasma proteins has been examined carefully with PAGE and immunochemical methods. The adsorption isotherms of albumin, fibrinogen, and IgG show a langmuir type adsorption. Delipidation of albumin did not alter the albumin affinity to Cuprophane and PVC. The surface saturation concentration (ng/cm2) for albumin, fibrinogen, or IgG were all found to be more on PVC (a hydrophobic surface) than on Cuprophane (a hydrophilic surface). The competitive adsorption of one protein species in a two- or three-protein mixture was also studied. Albumin and fibrinogen complete with each other for adsorption. The effects of IgG on the adsorption of albumin or fibrinogen were inconsistent and not predictable; the reason for this is unknown. The effect of laminar flow on albumin adsorption was studied with a specially designed Richardson flow chamber. In general caused an increase in albumin adsorption over that at static conditions. The increase of albumin adsorption was more pronounced also for PVC than for Cuprophane from 1 to 10 ml/min.
D000327:Adsorption; D001797:Blood Protein Electrophoresis; D001798:Blood Proteins; D004347:Drug Interactions; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen; D006801:Humans; D007074:Immunoglobulin G; D011108:Polymers; D011143:Polyvinyl Chloride; D012709:Serum Albumin; D012967:Sodium Dodecyl Sulfate; D014238:Trichloroacetic Acid
D001798:Blood Proteins; D007074:Immunoglobulin G; D011108:Polymers; D012709:Serum Albumin; D012967:Sodium Dodecyl Sulfate; D014238:Trichloroacetic Acid; D005340:Fibrinogen; D011143:Polyvinyl Chloride