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The purification and some properties of rhodanese from tortoise (Kinixys erosa, Schweigger) liver
Abstract
Rhodanese (cyanide: thiosulphate sulphur transferase; EC.2.8.1.1) was isolated from cytosolic fraction of tortoise liver using ammonium sulphate fractionation, ion exchange chromatography and gel filtration from the liver of tortoise. The enzyme had a specific activity of 14.43 RU per milligram of protein. The Km values for KCN and Na2S2O3 were 16 mM and 30.0 mM respectively. The native and subunit molecular weight of the enzyme was found to be 33,000 and 35,000 dalton respectively. The optimum pH and
temperature for the enzyme activity were 6.5 and 50 °C respectively. The enzyme was inhibited by Ba2+ and Zn2+ but not affected by Mn2+, Co2+
, Sn2+, Ni2+ and NH4 2+.
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Keywords: Rhodanese, tortoise, detoxification, sulphurtransferase enzyme, cyanide toxicity.
