Fournier D, Bride J M, Poirie M, Bergé J B, Plapp F W
Institut National de la Recherche Agronomique, Antibes, France.
J Biol Chem. 1992 Jan 25;267(3):1840-5.
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.
已从家蝇中鉴定并纯化出两类谷胱甘肽转移酶。第一类称为GST1,在SDS凝胶电泳中迁移为一条28 kDa的单带,第二类称为GST2,迁移为一条32 kDa的带。针对每一类制备的抗血清没有免疫交叉反应,并且未检测到两类之间的异二聚体关联。每一类都由几种同工型组成:GST1由等电点为4至9的形式组成,而GST2的所有形式都具有酸性pI值。对cDNA文库的筛选产生了编码GST1的克隆,该基因被测序并在大肠杆菌中表达。在抗杀虫剂品系(康奈尔R)中发现的高活性与高水平的GST1转录本相关。