A fibrinogen fragment D (D intermediate) with calcium binding but without anticlotting properties
article
Plasmin digestion of fibrinogen in the presence of Ca2+ or of EGTA leads to the formation of two sets of fragments, designated Dcate and D EGTA, respectively. Fragments Dcate, in contrast to D EGTA, bind one calcium ion and are anticlotting. Both these properties of Dcate are related to a 13-kDa carboxyl-terminal stretch of its ??-chain, which is missing in D EGTA. The molecular weights of the ??-chains of Dcate and D EGTA are 38000 and 25000, respectively. Now we have prepared a D-fragment, Dint, which has a ??-chain with a molecular weight of 29000. Dint binds one calcium ion per molecule but has no anticlotting properties. Thus the Ca2+-binding site of Dint (and Dcate) is directly dependent on the 4-kDa piece of the ??-chain that is present in Dint but not in D EGTA. As a consequence, the anticlotting properties of Dcate reside in the ?? 9-kDa stretch that is absent in Dint.
Chemicals/CAS: calcium, 7440-70-2; fibrinogen, 9001-32-5; plasmin, 9001-90-5, 9004-09-5; Calcium, 7440-70-2; Fibrin Fibrinogen Degradation Products; fibrinogen D fragment
Chemicals/CAS: calcium, 7440-70-2; fibrinogen, 9001-32-5; plasmin, 9001-90-5, 9004-09-5; Calcium, 7440-70-2; Fibrin Fibrinogen Degradation Products; fibrinogen D fragment
Topics
anticoagulant agentcalciumfibrinogenplasminblood and hemopoietic systemdrug bindingdrug mechanismdrug structurefibrinogen fragment dhumanhuman cellmetal bindingAmino Acid SequenceBlood CoagulationCalciumFibrin Fibrinogen Degradation ProductsHumanMolecular WeightProtein BindingSupport, Non-U.S. Gov't
TNO Identifier
229312
ISSN
00063002
Source
Biochimica et Biophysica Acta, 707(2), pp. 190-192.
Pages
190-192
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