The in vitro inhibitory effect on thrombin by 2,3-diphosphoglycerate.
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.
D000818:Animals; D000925:Anticoagulants; D001777:Blood Coagulation / Q000187:drug effects; D002417:Cattle; D002852:Chromatography, Ion Exchange / Q000379:methods; D003864:Depression, Chemical; D004163:Diphosphoglyceric Acids / Q000494:pharmacology*; D005337:Fibrin / Q000502:physiology; D005340:Fibrinogen / Q000502:physiology; D005344:Fibrinopeptide A / Q000037:antagonists & inhibitors; D005345:Fibrinopeptide B / Q000037:antagonists & inhibitors; D006801:Humans; D066298:In Vitro Techniques; D010447:Peptide Hydrolases / Q000097:blood; D013917:Thrombin / Q000037:antagonists & inhibitors*
D000925:Anticoagulants; D004163:Diphosphoglyceric Acids; D005344:Fibrinopeptide A; D005345:Fibrinopeptide B; D005337:Fibrin; D005340:Fibrinogen; D010447:Peptide Hydrolases; C023073:tosylarginine methyl ester hydrolase; D013917:Thrombin