In this paper, the adsorption of human serum albumin (HSA), human serum fibrinogen (HFG) and human serum immune globulin (IG) on surfaces of diamond like carbon film (DLC), diamond film (DF) and graphite has been studied. The adsorption isotherms of single component protein solution and the competitive adsorption of binary system have been investigated by radioisotope 125 I labeling method. Results showed that (1) the adsorptive amounts of HSA on DLC is more than that of HFG, but the adsorptive amounts of HFG on DF and graphite are apparently more than those HSA; (2) the relative competitive adsorption ability of three proteins on DF and graphite surfaces is HFG > IG > HSA, but that on DLC is HFG ≈ HAS > IG, comparison with HSA, there is no apparent competitive adsorption superiority on DLC for HFG. These results indicated that there is no apparent distinction for the adsorption of three human serum proteins on DLC, but the adsorption of HFG on DF and graphite takes precedence in varying degrees. It probably makes rational explanation for the result of blood-compatibility tests in vitro that DLC is good, but DF and graphite are worse.
