Showing results (21-30 of 475) with videos related to
Sort By:
Pageof 48
The Biochemical Journal|October 1, 1977
The involvement of the bridging imidazolate in the catalytic mechanism of action of bovine superoxide dismutaseM E McAdam, E M Feilden, F Lavelle, et al.European Journal of Biochemistry|August 1, 1975
Labile sulfur in human Superoxide dismutaseL Calabrese, G Federici, W H Bannister, et al.FEBS Letters|October 20, 1986
Primary structure of a cationic Cu,Zn superoxide dismutase. The sheep enzymeM E Schininà, D Barra, S Gentilomo, et al.Biochemical and Biophysical Research Communications|December 31, 1990
The Cu,Zn superoxide dismutase isoenzymes of Xenopus laevis: purification, identification of a heterodimer and differential heat sensitivityC R Capo, F Polticelli, L Calabrese, et al.The Biochemical Journal|April 1, 1974
Reduction and inactivation of superoxide dismutase by hydrogen peroxideR C Bray, S A Cockle, E M Fielden, et al.The Biochemical Journal|April 1, 1988
The effects of pH and various salts upon the activity of a series of superoxide dismutasesP O'Neill, S Davies, E M Fielden, et al.Archives of Biochemistry and Biophysics|July 1, 1994
Molecular modeling and electrostatic potential calculations on chemically modified Cu,Zn superoxide dismutases from Bos taurus and shark Prionace glauca: role of Lys134 in electrostatically steering the substrate to the active siteF Polticelli, M Falconi, P O'Neill, et al.The Biochemical Journal|April 1, 1974
Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysisE M Fielden, P B Roberts, R C Bray, et al.Biochemical and Biophysical Research Communications|July 15, 1988
Domains in bovine serum amine oxidaseA Giartosio, E Agostinelli, B MondoviArchives of Biochemistry and Biophysics|August 1, 1989
Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevisM E Schininà, D Barra, F Bossa, et al.Pageof 48