Abstract
Rhodanese, a cyanide detoxifying enzyme was extracted from the liver of Synodontis schall and its characteristics investigated. Crude enzyme preparation was prepared and the enzyme was assayed by measuring the activity of rhodanese in RU min-1 mg-1. The results revealed that rhodanese extracted from Synodontis schall liver had km values for Na2S2O3 and KCN were 12.23mM±1.36 and 8.45mM±1.05 respectively. The enzyme had higher affinity for KCN than Na2S2O3. Dithio oxiamide, 2-mercaptoethanol and sodium metabisulfite were not capable of replacing Na2S2O3 as sulfur donors. Na2S2O3 had the highest relative activity followed by ammonium sulphate. Synodontis schall liver rhodanese had optimum activity at pH 8.0 and 45ºC. Relative activities of cations tested showed that none had any significant effect on Synodontis schall liver rhodanese. Rhodanese present in the liver of Synodontis schall had properties similar to those from other sources.
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