Anticoagulant and calcium-binding properties of high molecular weight derivatives of human fibrinogen (plasmin fragments Y)

article


Nieuwenhuizen, W.

Voskuilen, M.

Hermans, J.
The present study was undertaken as a step to delineate further the localization of the calcium-binding sites in fibrinogen and to assess the anticlotting properties of fibrinogen degradation products. To this purpose, fragments Y were prepared by plasmin digestion of human fibrinogen in the presence of added Ca2+, and purified. We found that, on a molar basis, fragments Y exhibit twice as much anticlotting activity as fragments X. They possess two calcium-binding sites with K(d) = 1.9 x 10-5 M. Their predominant amino-terminal amino acids are alanine and tyrosine. It is known that one binding site in fragment Y is related to its D moiety. We conclude that the other calcium-binding site may be located in the central domain of the molecule.
Chemicals/CAS: alanine, 56-41-7, 6898-94-8; calcium, 7440-70-2; fibrinogen, 9001-32-5; plasmin, 9001-90-5, 9004-09-5; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; Calcium, 7440-70-2; Fibrin Fibrinogen Degradation Products; fibrinogen fragment Y; Fibrinogen, 9001-32-5; Plasmin, EC 3.4.21.7
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alanineanticoagulant agentcalciumfibrinogenfructose bisphosphateplasmintyrosineblood and hemopoietic systemdrug bindingdrug mechanismfragmentationhumanmetal bindingpharmacologystructure activity relationBinding SitesBlood CoagulationCalciumFibrin Fibrinogen Degradation ProductsFibrinogenHumanKineticsPlasminProtein BindingSupport, Non-U.S. Gov't
TNO Identifier
229282
Repository link
https://resolver.tno.nl/uuid:614ee218-fd0e-4c38-9169-da2993765d1a
ISSN
00063002
Source
Biochimica et Biophysica Acta, 708(3), pp. 313-316.
Pages
313-316
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