Rhodanese from Cercopithecus aethiops (vervet monkey) liver. I. Purification and some physical characteristics.
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 cation-exchange 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. The enzyme was physically characterized and its homogeneity determined by electrophoretic studies and gel chromatography. The rhodanese enzyme has a molecular weight of 37,000 daltons, a D020 ,w value of 7.6 X 10(-7) cm2 sec-1, a Stokes radius (molecular size) of 2.75 X 10(-7) cm and a frictional ratio of 1.071.
D000818:Animals; D002521:Cercopithecus / Q000378:metabolism*; D002522:Chlorocebus aethiops / Q000378:metabolism*; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D013466:Sulfurtransferases / Q000302:isolation & purification*; D013884:Thiosulfate Sulfurtransferase / Q000302:isolation & purification*
D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase