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Homology with hemopexin suggests a possible scavenging function for S‐protein/vitronectin
Author(s) -
Stanley K.K.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80489-6
Subject(s) - hemopexin , vitronectin , scavenging , homology (biology) , chemistry , function (biology) , biochemistry , biophysics , computational biology , biology , microbiology and biotechnology , gene , enzyme , heme , integrin , antioxidant , cell
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