Thromb Haemost 1987; 57(01): 073-076
DOI: 10.1055/s-0038-1651065
Original Articles
Schattauer GmbH Stuttgart

Zinc Alters Fibrin Ultrastructure

Gerard Marx
1   Department of Hematology, Beilinson Medical Center, Petah Tikva, Israel
,
Pierre Hopmeier
2   The Zentrallaboratorium, Krankenhaus Wien-Lainz, Vienna, Austria
,
Dorit Gurfel
3   The Department of Hematology, Hadassah University, Hospital, Jerusalem, Israel
› Author Affiliations
Further Information

Publication History

Received 12 August 1986

Accepted after revision 21 November 1986

Publication Date:
06 July 2018 (online)

Summary

Turbidimetric studies indicate that Zn(II) accelerates fibrin gelation [decreases clotting time (CT)] and increases maximal fibrin clot turbidity. For any given level of fibrinogen (0.2-2.6 mg/ ml), the relative fibrin turbidity of thrombin-induced clots increases with Zn(II) in a concentration dependent manner. Zinc-associated turbidity increases are also observed in the presence of 2 mM Ca(II). With citrate, similar turbidity increases are observed, though at higher cation levels. Thus, turbidimetry indicates that the gel formed with Zn(II) is coarser, or has thicker fibre strands. SEM micrographs confirm that fibre thickness ranges from 260 Å to 2600 Å, when Zn(II) levels range from 0-50 uM. With citrate, TEM micrographs reveal amore than 20 x fold increase in fibre diameter (100 Å->2000 Å) with higher Zn(II) (<1 mM) levels. Based on a fibrin monomer cross-section of ~60 Å, the electron micrographs indicate that depending on the Zn(II) levels, fibrin strands are composed of between 2 to 40 monomeric fibrin molecules. Thus, at physiologically relevant levels, Zn(II) can drastically modulate fibrin ultrastructure.