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.