Glutathione transferase from human erythrocytes: Nonidentity with the enzymes from liver
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2013, Journal of Molecular BiologyCitation Excerpt :Support for this interpretation was subsequently derived from equilibrium binding studies, which showed hyperbolic binding isotherms rather than cooperativity,4 but the true nature of the underlying mechanism remains unresolved. The human GST P1-1, first isolated from erythrocytes and placenta,5,6 was later studied and reported as showing Michaelis–Menten behavior7 but also as allosteric if the assay temperature was varied.8 In the present investigation, the elusive kinetic behavior of human GST P1-1 has been further probed by site-directed mutagenesis, insertion of unnatural amino acids, and inhibition studies.
FDA-approved drugs and other compounds tested as inhibitors of human glutathione transferase P1-1
2013, Chemico-Biological InteractionsCitation Excerpt :In human cells there are seven classes of soluble cytosolic GSTs (termed alpha, mu, pi, sigma, zeta, omega, and theta) occurring in dimeric forms [6]. One of the enzymes, GST P1-1, first isolated from erythrocytes [7] and placenta [8,9] is of particular interest since it is expressed at high levels in many tumor cell lines [10,11]. Its presence in drug-resistant tumors such as human malignant melanoma [12] and murine osteosarcoma [13] suggested that GST P1-1 could contribute to the resistance phenotype.
Differential expression of glutathione-S-transferase isoenzymes in various types of anemia in Taiwan
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Permanent address: Department of Biochemistry, The University of Tennessee, Center for the Health Sciences, Memphis, Tennessee 38163. This work was carried out at the National Institutes of Health under an Intergovernmental Personnel agreement with the University of Tennessee.