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Biochemistry|October 4, 1994
Contribution of amino acid residue 208 in the hydrophobic binding site to the catalytic mechanism of human glutathione transferase A1-1M Widersten, R Björnestedt, B MannervikThe Biochemical Journal|May 1, 1986
Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experimentsB Mannervik, I Jakobson, M WarholmFEBS Letters|January 21, 1985
The effect of 2,4,6-trinitrobenzenesulfonate on mercuric reductase, glutathione reductase and lipoamide dehydrogenaseI Carlberg, L Sahlman, B MannervikThe Biochemical Journal|March 1, 1979
Multiple inhibition of glutathione S-transferase A from rat liver by glutathione derivatives: kinetic analysis supporting a steady-state random sequential mechanismI Jakobson, M Warholm, B MannervikThe Journal of Biological Chemistry|August 10, 1979
The binding of substrates and a product of the enzymatic reaction to glutathione S-transferase AI Jakobson, M Warholm, B MannervikProtein Expression and Purification|June 1, 1996
Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNAM Widersten, M Huang, B MannervikBiochimica Et Biophysica Acta|September 18, 1981
Purification and immunological studies of glutathione reductase from rat liver. Evidence for an antigenic determinant at the nucleotide-binding domain of the enzymeI Carlberg, B Altmejd, B MannervikEuropean Journal of Biochemistry|October 1, 1976
Error structure of enzyme kinetic experiments. Implications for weighting in regression analysis of experimental dataP Askelöf, M Korsfeldt, B MannervikBiochimica Et Biophysica Acta|December 8, 1978
Characterization of glutathione reductase from porcine erythrocytesV Boggaram, K Larson, B MannervikFEBS Letters|March 25, 1985
Structural evidence for three different types of glutathione transferase in human tissuesP Alin, B Mannervik, H JörnvallPageof 22