gamma-dimerization, alpha-polymerization, and plasmin degradation of human fibrin. Effect of various inhibitors of factor XIII on the patterns in SDS-electrophoresis and crossed immunoelectrophoresis.
The effect of different factor XIII inhibitors (competetive inhibition, interference with active center SH-groups in different ways, Ca2+ depletion) on the sequence of the gamma-dimerization and alpha-polymerization of fibrin is examined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAE) (reduced material). They all inhibit either gamma-dimerization and alpha-polymerization or alpha-polymerization alone irrespective of the factor XIII inhibitory mechanism. Non-crosslinked fibrin and fibrin clots of different degrees of crosslinking are digested with plasmin and the lysate tested in SDS-PAE (non-reduced material) and crossed agarose gel immunoelectrophoresis (CAIE). The digests contain Fragment D and Fragment D-D respectively and Fragment E. An additional Fragment E with less anodic mobility in CAIE, and not demonstrable in SDS-PAE, is seen in increasing amounts with increasing gamma-dimerization, alpha-polymerization does not further change the CAIE patterns.
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005176:Factor XIII / Q000037:antagonists & inhibitors*; D005337:Fibrin / Q000378:metabolism*; D005341:Fibrinolysin; D006801:Humans; D007122:Immunoelectrophoresis; D011108:Polymers; D012967:Sodium Dodecyl Sulfate; D013552:Swine
D011108:Polymers; D012967:Sodium Dodecyl Sulfate; D005337:Fibrin; D005176:Factor XIII; D005341:Fibrinolysin