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

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Author: Nieuwenhuizen, W. · Voskuilen, M. · Hermans, J.
Institution: Gaubius instituut TNO
Source:Biochimica et Biophysica Acta, 3, 708, 313-316
Identifier: 229282
Keywords: Biology · alanine · anticoagulant agent · calcium · fibrinogen · fructose bisphosphate · plasmin · tyrosine · blood and hemopoietic system · drug binding · drug mechanism · fragmentation · human · metal binding · pharmacology · structure activity relation · Binding Sites · Blood Coagulation · Calcium · Fibrin Fibrinogen Degradation Products · Fibrinogen · Human · Kinetics · Plasmin · Protein Binding · Support, Non-U.S. Gov't


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