Thromb Haemost 1976; 36(01): 027-036
DOI: 10.1055/s-0038-1648006
Original Article
Schattauer GmbH

γ-Dimerization, α-Polymerization, and Plasmin Degradation of Human Fibrin

Effect of Various Inhibitors of Factor XIII on the Patterns in SDS-Electrophoresis and Crossed Immunoelectrophoresis
J Carsten Feddersen
1  Coagulation Laboratory, Sundby Hospital, DK-2300 Copenhagen S, Denmark
,
Johs Gormsen
1  Coagulation Laboratory, Sundby Hospital, DK-2300 Copenhagen S, Denmark
› Author Affiliations
Further Information

Publication History

Received 25 June 1975

Accepted 06 March 1976

Publication Date:
03 July 2018 (online)

Summary

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 γ-dimerization and α-polymerization of fibrin is examined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAE) (reduced material). They all inhibit either γ-dimerization and a-polymerization or a-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 γ-dimerization, α-polymerization does not further change the CAIE patterns.