Print Email Facebook Twitter Anticoagulant and calcium-binding properties of high molecular weight derivatives of human fibrinogen (plasmin fragments Y) Title Anticoagulant and calcium-binding properties of high molecular weight derivatives of human fibrinogen (plasmin fragments Y) Author Nieuwenhuizen, W. Voskuilen, M. Hermans, J. Gaubius instituut TNO Publication year 1982 Abstract 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 126.96.36.199 Subject Biologyalanineanticoagulant agentcalciumfibrinogenfructose bisphosphateplasmintyrosineblood and hemopoietic systemdrug bindingdrug mechanismfragmentationhumanmetal bindingpharmacologystructure activity relationBinding SitesBlood CoagulationCalciumFibrin Fibrinogen Degradation ProductsFibrinogenHumanKineticsPlasminProtein BindingSupport, Non-U.S. Gov't To reference this document use: http://resolver.tudelft.nl/uuid:614ee218-fd0e-4c38-9169-da2993765d1a TNO identifier 229282 ISSN 0006-3002 Source Biochimica et Biophysica Acta, 708 (3), 313-316 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.