Generation of the combined prothrombin activation peptide (F1-2) during the clotting of blood and plasma.
Open Access
- 1 December 1977
- journal article
- research article
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 60 (6) , 1410-1418
- https://doi.org/10.1172/jci108902
Abstract
We have investigated the pathway of prothrombin activation in blood and plasma. By means of a rapid purification procedure involving chromatography on DEAE-cellulose and hydroxyapatite, we demonstrated that the major prothrombin fragment in serum is that representing the amino-terminal half of prothrombin (i.e. F1-2). The F1-2 isolated was characterized by its size, amino acid and antigenic compositions, amino-terminal residue, and the peptides (designated F1 and F2, respectively) it yielded upon hydrolysis by thrombin. Measurements by the isotope dilution technique showed that F1-2 could account for the fate of at least 90% of the prothrombin originally present in plasma. By contrast, the serum concentration of the fragment representing the amino-terminal third of prothrombin (viz. F1) was less than 10% that of F1-2. These results demonstrated that the major route of prothrombin conversion in blood or plasma involves the removal of the combined activation fragment (F1-2) as a single peptide.This publication has 20 references indexed in Scilit:
- The conversion of prothrombin to thrombin. III. The factor Xa-catalyzed activation of prothrombin.1974
- The conversion of prothrombin to thrombin. V. The activation of prothrombin by factor Xa in the presence of phospholipid.1974
- The conversion of prothrombin to thrombin. II. Differentiation between thrombin- and factor Xa-catalyzed proteolyses.1974
- The Essential Covalent Structure of Human Fibrinogen Evinced by Analysis of Derivatives Formed during Plasmic HydrolysisJournal of Biological Chemistry, 1973
- Studies on the chemical and enzymatic modification of glycoproteins. A general method for the tritiation of sialic acid-containing glycoproteins.1971
- The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel ElectrophoresisJournal of Biological Chemistry, 1969
- Prothrombin Fragmentation During Coagulation of Whole Blood and PlasmaScandinavian Journal of Clinical and Laboratory Investigation, 1969
- ON OCCURRENCE OF POLYMORPHIC HUMAN PROTHROMBIN - ELECTROPHORETIC AND CHROMATOGRAPHIC ALTERATIONS OF MOLECULE DUE TO ACTION OF THROMBIN1968
- Chromatographic Analysis of the Activation of Human Prothrombin with Human Thrombokinase*Biochemistry, 1966
- The Specific Assay of Prower-Stuart Factor and Factor VIIActa Haematologica, 1961