Clotting of fibrinogen. 2. Calorimetry of the reversal of the effect of calcium on clotting with thrombin and with Ancrod
- 1 July 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (14) , 3443-3448
- https://doi.org/10.1021/bi00335a008
Abstract
When clotting is effected by thrombin in the presence of Ca, the endotherm for the D nodules of fibrinogen broadens significantly and then becomes narrow again, while increasing in size. Clotting effected by the snake venom enzyme, Ancrod, which releases only the A fibrinopeptides from the E nodule, shows only the broadening of the D endotherm. Accordingly, significant interactions of the D nodules of fibrinogen become possible only when the B fibrinopeptides of the E nodule are released on clotting. When Ca present during clotting is removed from the fibrin clot with ethylenediaminetetraacetic acid, the endotherm for the D nodules of fibrin shows nearly complete reversal if clotting was effected with Ancrod but appears to be divided into 2 endotherms if clotting was effected with thrombin. At neutral pH, new endotherms were observed for fibrinogen in the temperature range 105-140.degree. C.This publication has 5 references indexed in Scilit:
- Clotting of fibrinogen. 1. Scanning calorimetric study of the effect of calciumBiochemistry, 1985
- Domains in the fibrinogen moleculeJournal of Molecular Biology, 1982
- COMPARISON OF POLYMERIZATION OF ANCROD AND THROMBIN FIBRIN MONOMERS1977
- Physicochemical studies of bovine fibrinogen III. Optical rotation of the native and denatured moleculeBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965
- The Fibrinogen Molecule: Its Size, Shape, and Mode of PolymerizationThe Journal of cell biology, 1959