Zinc binding to fibrinogen and fibrin.

Article Details

Citation

Marx G

Zinc binding to fibrinogen and fibrin.

Arch Biochem Biophys. 1988 Oct;266(1):285-8.

PubMed ID
3178229 [ View in PubMed
]
Abstract

Zinc binding to fibrinogen and fibrin was studied by two techniques. Scatchard analysis of ultrafiltration eluates reveals that fibrinogen has multiple Zn(II)-binding sites, KD (fibrinogen) = 18 microM; n = 6. The zinc content of the "collapsed" fibrin gel supernatant was also determined by atomic absorption spectroscopy and analyzed by a Scatchard plot (KD (fibrin) = 8 microM, n = 6). In other experiments, Zn(II) did not displace 45Ca(II) from fibrin. It appears that the binding of zinc to fibrinogen or fibrin is distinct from that of calcium, and that the zinc-binding characteristics of fibrinogen and fibrin are not significantly affected by the transformation of one into the other.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
ZincFibrinogen alpha chainProteinHumans
Unknown
Not AvailableDetails
Zinc acetateFibrinogen alpha chainProteinHumans
Unknown
Not AvailableDetails
Zinc chlorideFibrinogen alpha chainProteinHumans
Unknown
Binder
Details
Zinc sulfate, unspecified formFibrinogen alpha chainProteinHumans
Unknown
Binder
Details