About 80% of thrombin was inactivated after 50 minutes chemical reduction at 22°C in a reaction mixture containing 0.1 M mercaptoethanol and 2.6 M urea. The reduced protein was spontaneously reoxidated in air at 22°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.
|Number of pages||5|
|Journal||Acta physiologica Academiae Scientiarum Hungaricae|
|Publication status||Published - dec. 1 1978|
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