Glutathione S-aralkyltransferase

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Glutathione S-aralkyltransferase.

1. The name ;glutathione S-aralkyltransferase' is proposed for the enzyme catalysing the reaction of benzyl chloride with GSH. 2. Results from heat-inactivation studies, ammonium sulphate-fractionation and acid-precipitation experiments, and studies of the distribution of activities in rat liver, in rat kidney and in the livers of other animals indicate that glutathione S-aralkyltransferase dif...

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Class-Pi of Glutathione S-Transferases

Class-Pi of glutathione s-transferases (GST-Pi) is the specific form of GSTs that are known to participate particularly in the mechanisms of resistance to drugs and carcinogens. This class of the enzyme is referred to as class-P or class-Pi or class π. The accepted terminology in this review article is class-Pi. In this article following a brief description of identified molecular forms of GSTs...

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Glutathione S-transferases Null Genotype in Acute Myeloid Leukaemia

Background: The glutathione S-transferase (GST) family of metabolising enzymes plays an important role in the detoxification of mutagens and carcinogens. The expression of many of these cancer susceptibility enzymes is genetically polymorphic. An increased frequency of GST-null genotypes has been associated with several malignancies. Objective: To investigate the rate of GSTT1 and GSTM1 null ge...

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Human intestinal glutathione S - transferases

Cytosolic glutathione S-transferases were purified from the epithelial cells of human small and large intestine. These preparations were characterized with regard to specific activities, subunit and isoenzyme composition. Isoenzyme composition and specific activity showed little variation from proximal to distal small intestine. Specific activities of hepatic and intestinal enzymes from the sam...

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Mouse Liver Glutathione S-Transferases

Three major forms of cytosolic glutathione S-transferase (designated F1, F2, and F3 transferases according to increasing isoelectric points) were purified to homogeneity from liver of DBA/2J mice, primarily by CM-cellulose and hydroxylapatite chromatography. The purified enzymes were shown to have specific activities of 104, 281, and 143 units/mg, respectively, when assayed with 1 m~ each of l-...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1969

ISSN: 0306-3283

DOI: 10.1042/bj1150985