The in vitro inhibitory effect on thrombin by 2,3-diphosphoglycerate

Autor:	D, Del Principe, P M, Strappini, S, Del Vecchio, A, Menichelli, G, Biancini, E V, Cosmi, V, Bastianon, C, D'Arcangelo
Rok vydání:	1981
Předmět:	Fibrin Thrombin Anticoagulants Fibrinogen In Vitro Techniques Chromatography Ion Exchange Diphosphoglyceric Acids Depression Chemical Animals Humans Cattle Blood Coagulation Fibrinopeptide B Fibrinopeptide A Peptide Hydrolases
Zdroj:	Thrombosis and haemostasis. 46(3)
ISSN:	0340-6245
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::9069269b32a7061db37100c7be0cb5c5 https://pubmed.ncbi.nlm.nih.gov/7031980 Zobrazit plný text záznamu