Related Experiment Video
Updated: Aug 8, 2026

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance
Published on: October 16, 2018
Homology with hemopexin suggests a possible scavenging function for S-protein/vitronectin
S-protein is an abundant plasma protein which has recently been shown to be identical to vitronectin and serum spreading factor [(1985) EMBO J. 4, 3153-3157]. It therefore has multiple binding sites for terminal complement complexes, thrombin-antithrombin III, heparin, and a specific cell receptor. In this report a structural and sequence homology with hemopexin is described which suggests that the principle function of S-protein could be as a scavenging molecule, clearing spent complement and coagulation complexes from the circulation.
S-protein is an abundant plasma protein which has recently been shown to be identical to vitronectin and serum spreading factor [(1985) EMBO J. 4, 3153-3157]. It therefore has multiple binding sites for terminal complement complexes, thrombin-antithrombin III, heparin, and a specific cell receptor. In this report a structural and sequence homology with hemopexin is described which suggests that the principle function of S-protein could be as a scavenging molecule, clearing spent complement and coagulation complexes from the circulation.
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