Effects of certain purified plasma proteins on the compatibility of glass with blood

Abstract

The effects of certain purified plasma proteins on the coagulation-activation and platelet-adhesion properties of glass surfaces have been investigated. Albumin, transferrin, gammaG globulin, gammaM globulin and fibrinogen were obtained in highly purified form; ceruloplasmin was a more crude preparation. Each of these proteins was found to adhere to glass surfaces and influence reactions of these surfaces with blood. gammaG globulin or albumin adsorbed to glass markedly inhibited activation of the intrinsic coagulation system, while the other proteins tested were much less effective in this respect. Fibrinogen, of all the proteins tested, greatly enhanced the adhesion of platelets to glass. Albumin, ceruloplasmin, transferrin, gammaG globulin and gammaM globulin each decreased the adhesion of platelets to glass by approximately 50%. Ultrastructural studies of the interface area where blood reacted with the layer of protein adsorbed to glass demonstrated the deposition of a moderately thick irregular protein layer upon the surface, with adhesion of cellular elements to this unilaminar adsorbed layer. Ultrastructural studies also demonstrated that platelets which adhere to protein-coated surfaces formed pseudopods and spread upon such surfaces.