Air reoxidation and reactivation of reduced thrombin.
About 80% of thrombin was inactivated after 50 minutes chemical reduction at 22 degrees C in a reaction mixture containing o.1 M mercaptoethanol and 2.6 M urea. The reduced protein was spontaneously reoxidated in air at 22 degrees C in 30--60 minutes. The reoxidation of disulphide bonds in thrombin led to partial reactivation of the enzyme. Recovery of thrombin activity after oxidation ranged from 0 to 60% according to the conditions of reoxidation in air. Heparin and copper ion increased the rate of reactivation, whereas in the presence of 10 mM iodoacetamide there was no reactivation.
D000388:Air; D003300:Copper / Q000494:pharmacology; D004789:Enzyme Activation; D006493:Heparin / Q000494:pharmacology; D007460:Iodoacetamide / Q000494:pharmacology; D010084:Oxidation-Reduction; D013431:Sulfates / Q000494:pharmacology; D013917:Thrombin
D013431:Sulfates; D003300:Copper; D006493:Heparin; D013917:Thrombin; D007460:Iodoacetamide