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Title of Journal: Parasitol Res

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Abbravation: Parasitology Research

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Springer-Verlag

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DOI

10.1007/s10661-007-9926-5

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1432-1955

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Biochemical studies on glutathione Stransferase f

Authors: Lakshmy Srinivasan Nisha Mathew Twinkle Karunan Kalyanasundaram Muthuswamy
Publish Date: 2011/01/05
Volume: 109, Issue: 1, Pages: 213-219
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Abstract

Setaria digitata is a filarial worm of the cattle used as a model system for antifilarial drug screening due to its similarity to the human filarial parasites Wuchereria bancrofti and Brugia malayi Since filarial glutathione Stransferase GST is a good biochemical target for antifilarial drug development a study has been undertaken for the biochemical characterization of GST from S digitata Cytosolic fraction was separated from the crude Sdigitata worm homogenate by ultracentrifugation at 100000 g and subjected to ammonium sulfate precipitation followed by affinity chromatography using GSHagarose column The kinetic parameters Km and Vmax values with respect to GSH were 045 mM and 0105 μmol min−1 mL1 respectively With respect to 1chloro24dinitrobenzene the Km and Vmax values were 121 and 0117 μmol min−1 mL−1 respectively The effect of temperature and pH on GST enzyme activity was studied The protein retained its enzyme activity between 0°C and 40°C beyond which it showed a decreasing tendency and at 80°C the activity was lost completely The enzyme activity was varying with change in pH and the maximum GST activity was observed at pH 75 Gel filtration chromatographic studies indicated that the protein has a native molecular mass of about 54 kDa The single band of GST subunit appeared in sodium dodecyl sulfate polyacrylamide gel electrophoresis was found to have molecular mass of ∼27 kDa This shows that cytosolic S digitata GST protein is homodimeric in nature

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