The effect of fibrin-stabilizing factor on the subunit structure of human fibrin.
The formation of human fibrin from fibrinogen has been examined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, a method which separates a mixture of proteins on the basis of differences in molecular weight. It has been found that the plasma from a patient with a congenital deficiency of fibrin-stabilizing factor forms clots lacking the cross links among the alpha- and gammachains found in normal, cross-linked human fibrin. The addition of purified fibrin-stabilizing factor or normal plasma to the deficient plasma results in extensive cross-linking of the chains. Thus, the fibrinogen in the fibrin-stabilizing factor deficient plasma appears to be normal and forms fibrin which contains dimeric, cross-linked gamma-chains and polymeric, high molecular weight forms of alpha-chains. By the use of these electrophoretic methods, it has also been possible to develop a highly sensitive method for measuring the content of fibrin-stabilizing factor in plasma. This method depends upon the use of urea-treated fibrinogen, which is completely devoid of fibrin-stabilizing factor, but which forms the usual cross-linked subunits after conversion to fibrin by thrombin in the presence of fibrin-stabilizing factor.
D000085:Acetates; D001778:Blood Coagulation Disorders / Q000097:blood; D001797:Blood Protein Electrophoresis; D005033:Ethylmaleimide; D005176:Factor XIII; D005337:Fibrin; D005340:Fibrinogen; D006146:Guanidines; D006801:Humans; D008722:Methods; D008970:Molecular Weight; D014508:Urea
D000085:Acetates; D006146:Guanidines; D014508:Urea; D005337:Fibrin; D005340:Fibrinogen; D005176:Factor XIII; D005033:Ethylmaleimide