The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Increased synthesis of glutathione S-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA.

Glutathione S-transferase activities in mouse hepatic cytosols are elevated as much as 11-fold following the administration of BHA (2(3)-tert-butyl-4-hydroxyanisole), a widely used antioxidant food additive. Ethoxyquin (1,2-dihydro-6-ethoxy-2,2,4-trimethylquinoline) and disulfiram [bis(diethyldithiocarbamyl)disulfide] also enhance the activities of glutathione S-transferases and certain other enzymes. Each of these compounds protects rodents against mutagenic and carcinogenic metabolites. A major (pI 8.7) and a minor (pI 9.3) component of the family of mouse hepatic glutathione S-transferases have been purified to homogeneity. These transferases are immunologically cross-reactive, and have a high degree of NH2-terminal sequence homology (but are not identical). The enzymes differ in a number of molecular and catalytic properties. The transferases are 12-fold elevated by dietary BHA as demonstrated by immunotitration. The mRNA for the major glutathione S-transferase is increased more than 20-fold in the liver RNA of BHA-fed mice, as determined by translation of total liver mRNA and characterization of the products by immunoprecipitation and sodium dodecyl sulfate-gel electrophoresis or by two-dimensional gel electrophoresis. A cDNA plasmid complementary to glutathione S-transferase mRNA was constructed. Translation of liver mRNA selected by hybridization with this plasmid gave products similar to or identical with glutathione S-transferase polypeptides. The cDNA insert has been partially sequenced and its orientation has been determined. Its sequence corresponds to the NH2-terminal region (beginning at residue 9) of the amino acid sequence of the glutathione S-transferase with pI 9. 3. Hybridization of the 32P-labeled cDNA plasmid with total liver RNA indicates a 26-fold increase in homologous mRNA in response to the feeding of BHA.[1]

References

  1. Increased synthesis of glutathione S-transferases in response to anticarcinogenic antioxidants. Cloning and measurement of messenger RNA. Pearson, W.R., Windle, J.J., Morrow, J.F., Benson, A.M., Talalay, P. J. Biol. Chem. (1983) [Pubmed]
 
WikiGenes - Universities