title: Phosphorylation of complement factor C3 in vivo.
abstract: Complement factor C3, the central protein of the complement system, was found to be phosphorylated both in EDTA- and heparin-anticoagulated whole blood and in coagulating blood. Complement S protein (vitronectin) was also found to be phosphorylated under these conditions. Further, purified C3 was found to be a phosphoprotein in vivo, containing 0.15 mol of alkali-labile phosphate/mol of protein. The ATP concentration in plasma was measured and found to be about 2 microM.
authors: Department of Medical and Physiological Chemistry, Uppsala University, Sweden.
authors: S C
authors: SC
authors: Martin
mesh_terms: D000255:Adenosine Triphosphate / Q000097:blood; D001798:Blood Proteins / Q000378:metabolism; D003176:Complement C3 / Q000378:metabolism*; D006023:Glycoproteins / Q000097:blood; D006801:Humans; D010766:Phosphorylation; D011233:Precipitin Tests; D011494:Protein Kinases / Q000097:blood; D019096:Vitronectin
chemical_list: D001798:Blood Proteins; D003176:Complement C3; D006023:Glycoproteins; D019096:Vitronectin; D000255:Adenosine Triphosphate; D011494:Protein Kinases