Abstract
1. 1. Rhodanese (thiosulphate sulphurtransferase, EC 2.8.1.1.) from Cercopithecus aethiops (vervet monkey) liver has been isolated and purified by means of extraction, ammoniumsulphate and pH fractionation, anion-exchange chromatography, Sephacryl S-300 gel chromatography and cationexchange chromatography. A yield of about 10% pure enzyme with a specific activity of 242 U/mg protein corresponding to a purification factor of 523 was obtained. 2. 2. The enzyme was physically characterized and its homogeneity determined by electrophoretic studies and gel chromatography. 3. 3. The rhodanese enzyme has a molecular weight of 37,000 daltons, a D 20,w 0 value of 7.6 × 10 −7 cm 2 sec t1̄, a Stokes radius (molecular size) of 2.75 × 10 −7 cm and a frictional ratio of 1.071.
Published Version
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