Physicochemical, immunochemical and functional comparison of human S-protein and vitronectin. Evidence for the identity of both plasma proteins

Abstract

The comparison of the complement inhibitor s-protein, isolated from human plasma, with vitronectin, a serum spreading factor, revealed a high degree of similarity of both proteins with respect to molecular weight, band pattern in polyacrylamide gels in the presence of sodium dodecyl sulfate and amino acid composition. While radiolabeled S-protein was precipitated by antiserum against vitronectin, both proteins exhibited precipitin lines of complete identity in double immunodiffusion analysis when tested mutually against antisera of the appropriate components. The functional property of vitronectin to promote cell spreading of fibroblasts was also documented for purified S-protein. These findings indicate a high degree of similarity with respect to structural and functional properties of S-protein and vitronectin and hence may implicate that both proteins are identical.