title: Zinc binding to fibrinogen and fibrin.
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.
authors.affiliation: Coagulation Laboratory, Magen David Adom Blood Services, Tel Hashomer, Israel.
authors.forename: G
authors.initials: G
authors.lastname: Marx
mesh_terms: D002118:Calcium / Q000378:metabolism; D002413:Cations, Divalent; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D011485:Protein Binding; D015032:Zinc / Q000378:metabolism*
chemical_list: D002413:Cations, Divalent; D005337:Fibrin; D005340:Fibrinogen; D015032:Zinc; D002118:Calcium