Student Research: Mary Trute
The glutathione S-transferases (GSTs) are a phase II detoxification enzyme family that can mitigate the cellular toxicity of a number of endogenous and environmental chemicals. GSTs arise from several gene families and encode dimeric proteins that include cytocolic, mitochondrial, and microsomal isoforms (Hayes and Pulford, 1995). At present, GST isoforms in mammals comprise at least 8 classes based on primary amino acids sequence and include; alpha, mu, pi, sigma, theta, omega, kappa, and zeta GSTs. Although no clearly established criteria exist for assigning a GST to a particular class, it is generally accepted that GST sharing more than 40% identify are assigned to the same class, and those sharing less than 30% would be assigned to different classes (Hayes and Pulford, 1995). The mircrosomal GST isoforms constitute a separate gene family and have been recently designated membrane associated proteins involved in eicosanoid and gluthathione (GSH) metabolism (MAPEG) proteins (Hayes, Flanagan, and Jowsey, 2005).
Taken from the beginning of thesis.