The in vitro inhibitory effect on thrombin by 2,3-diphosphoglycerate
Del Principe, D.; Strappini, P.M.; Del Vecchio, S.; Menichelli, A.; Biancini, G.; Cosmi, E.V.; Bastianon, V.; D'Arcangelo, C.
Thrombosis and Haemostasis 46(3): 581-583
1981
ISSN/ISBN: 0340-6245 PMID: 7031980 Document Number: 169796
Thrombin incubated with 2,3-diphosphoglycerate (150 nmol 2,3-DPG/1 NIH thrombin unit) lost up to 70% of its clotting activity, whereas the esterase activity remained unchanged. No fibrinopeptide release by thrombin was observed in the presence of 2,3-DPG. The fibrin polymerization was normal. By chromatography on Amberlite IRC-50, alpha-thrombin was eluted at pH 8.0. In presence of 2,3-DPG, alpha-thrombin was not eluted. Likely, 2,3-DPG can interfere with thrombin.