Biochemical characterization of Drosophila glutathione S-transferases D1 and D21.
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چکیده
منابع مشابه
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...
متن کاملMolecular evolution of glutathione S-transferases in the genus Drosophila.
As classical phase II detoxification enzymes, glutathione S-transferases (GSTs) have been implicated in insecticide resistance and may have evolved in response to toxins in the niche-defining feeding substrates of Drosophila species. We have annotated the GST genes of the 12 Drosophila species with recently sequenced genomes and analyzed their molecular evolution. Gene copy number variation is ...
متن کاملGlutathione 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...
متن کاملRat lung glutathione S - transferases
Two immunologically distinct types of 22000-Mr subunits are present in rat lung glutathione S-transferases. One of these subunits is probably similar to Ya subunits of rat liver glutathione S-transferases, whereas the other subunit Ya' is immunologically distinct. Glutathione S-transferase II (pI7.2) of rat lung is a heterodimer (YaYa') of these subunits, and glutathione S-transferase VI (pI4.8...
متن کاملHuman 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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)46868-8