Protein Technology Topics: Determination of Glutathione-S-Transferase Activity

Glutathione S-transferase refers to an enzyme that catalyzes the reaction of an exogenous compound having an electrophilic substituent with endogenous reduced glutathione (GSH). A variety of reactions can be catalyzed including the transfer of a hydrocarbyl group, an aryl group, an aromatic hydrocarbon group, an alkenyl group, and an oxy group.
Glutathione S-transferase is a key enzyme in the glutathione binding reaction, and the initial step of catalyzing the glutathione binding reaction is mainly in the cytosol. Glutathione S-transferase can be divided into the following five types depending on the substrate to be used:
1. Glutathione S-transalkylase: catalyzes the glutathione binding reaction of an alkyl halide and a nitroalkane compound. Mainly in the liver and kidneys.
2. Glutathione S-aryltransferase: mainly catalyzes the glutathione binding reaction of aromatic hydrocarbons or other cyclic compounds containing a halogen group or a nitro group, such as bromobenzene and organophosphorus insecticides. This enzyme is mainly found in liver cytosol.
3. Glutathione S-aralkyltransferase: Catalyzed glutathione binding reaction of an aralkyl group, for example, an aralkyl halide such as benzyl chloride. Mainly in the liver and kidneys.
4. Glutathione S-epoxide transferase: Catalyzes the binding of epoxide derivatives of aromatic hydrocarbons and halogenated benzenes to glutathione, mainly in liver and kidney cytosol.
5. Glutathione S-olefin transferase: catalyzes the binding reaction of unsaturated olefinic compounds containing α,β-unsaturated carbonyl groups to glutathione, mainly in liver and kidney cytosol.
Glutathione S-transferase is of toxicological importance. It catalyzes the binding reaction of nucleophilic glutathione to various electrophilic exogenous chemicals. Many exogenous chemicals are highly susceptible to the formation of certain biologically active intermediates in the first phase reaction of biotransformation, which can covalently bind to important components of cellular biomacromolecules and cause damage to the organism. When glutathione is combined with it, it can prevent such covalent binding and detoxification.

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