[The effect of dithiothreitol on the thrombin coagulating activity].
Partial dithiothreitol-reduction of the disulphide thrombin bonds when denaturating agents are absent lowers significantly enzymic activity of thrombin relative to fibrinogen coagulation. This permits supposing that at least one of the disulphide bridges in a thrombin molecule is necessary for stabilization of the space structure important for a specific hydrolysis of fibrinogen.
D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects*; D002417:Cattle; D004229:Dithiothreitol / Q000494:pharmacology*; D007700:Kinetics; D011487:Protein Conformation / Q000187:drug effects; D013696:Temperature; D013917:Thrombin / Q000032:analysis / Q000037:antagonists & inhibitors* / Q000502:physiology
D013917:Thrombin; D004229:Dithiothreitol
Vliianie ditiotreitola na svertyvaiushchuiu aktivnost' trombina.