title: Coagulation proteins showing abnormal electrophoretic mobility in commercial concentrates of factor VIII and prothrombin complex.
abstract: Five commercial factor VIII (FVIII) concentrates and three prothrombin complex concentrates (PCC) were studied with reference to the qualitative evaluation of factors II, IX, fibronectin, alpha 2-antiplasmin (alpha 2-AP), antithrombin III (AT-III) and subunits A and S of FXIII by crossed-immunoelectrophoresis (CIE) and von Willebrand factor antigen (vWF:Ag) by radio-CIE. This latter protein had a different pattern with the absence or a decrease of larger forms and the presence of a fast-moving precipitating peak, suggesting degradation of the vWF:Ag in FVIII concentrates. In contrast, the electrophoretic mobility of fibronectin, alpha 2-AP and AT-III was normal. All PCC showed a more anodic mobility of factor IX. alpha 2-AP also exhibited a different electrophoretic pattern to that of normal plasma. Abnormality of AT-III was also found in heparin-binding studies. The techniques used in the purification procedures are probably the mechanism responsible for the partial denaturing of these proteins.
mesh_terms: D000990:Antithrombin III / Q000032:analysis; D001779:Blood Coagulation Factors / Q000032:analysis* / Q000302:isolation & purification / Q000592:standards; D001797:Blood Protein Electrophoresis; D003378:Counterimmunoelectrophoresis; D004340:Drug Contamination; D005169:Factor VIII / Q000032:analysis* / Q000302:isolation & purification / Q000592:standards; D005353:Fibronectins / Q000032:analysis; D006801:Humans; D011489:Protein Denaturation
chemical_list: D001779:Blood Coagulation Factors; D005353:Fibronectins; C025667:prothrombin complex concentrates; D000990:Antithrombin III; D005169:Factor VIII