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Background: 3-Mercaptopyruvate sulfurtransferase (3-MST) is a multifunctional, mitochondrial and cytoplasmic sulphurtransferase that catalyses the detoxification of cyanide to a less toxic thiocyanate. Limicolaria flammea feeds majorly on green leaves, plants and other cyanide containing foods. Methods: 3-MST from the hemolymph of Limicolaria flammae was purified by 70 % ammonium sulphate precipitation and ion exchange chromatography. The purified enzyme was characterized at different levels such as optimal activity, inhibitors, substrate preference, thermal stability and analysis of ki-

pan african journal of life sciences

Physicochemical Properties of 3-Mercaptopyruvate Sulfurtransferase: A Cyanide Detoxifying Enzyme from the Hemolymph of Limicolaria flammae (Garden Snail)