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Two classes of glutathione transferases have been identified and purified from Musca domestica. The first, designated as GST1, migrates as a single band of 28 kDa in SDS-gel electrophoresis, and the second, designated as GST2, migrates as a 32-kDa band. Antisera prepared against each class have no immunological cross-reactivity, and heterodimeric associations between the two classes have not been detected. Each class is composed of several isoforms: GST1 is composed of forms with isoelectric points from 4 to 9, whereas all the forms of GST2 have acidic pI values. Screening of cDNA libraries yielded clones coding for GST1, and the gene was sequenced and expressed in Escherichia coli. The high activity found in an insecticide-resistant strain (Cornell R) is correlated with high level of GST1 transcript.
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Fournier et al. (1992) studied this question.
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