Abstract
Publisher Summary This chapter focuses on the purification of soluble human glutathione S-transferases. Soluble glutathione transferases (GSTs) catalyze glutathione-dependent nucleophilic substitution and addition reactions with endogenous and xenobiotic electrophiles as well as the reduction of hydroperoxides, quinones, and quinoneimines. The human kidney is a good source of GSTPI-I but also contains alpha class GSTs together with small amounts of mu class GSTs, including M3-3. The procedure is very similar to that for the liver GSTs with the following modifications. The soluble fraction from 40 g of kidney is applied to the 40-ml affinity column. The concentration of GSTs in skeletal muscle is in the region of 4% that of the liver. However, because skeletal muscle accounts for 40% of body mass, the total hepatic and skeletal muscle GST activities are similar. Skeletal muscle is a very important component of extrahepatic GST activity. Enzyme purity may be assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), isoelectrofocusing, and reversedphase high-performance liquid chromatography (HPLC).
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