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E Argese

Showing results (1-10 of 11) with videos related to

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The Biochemical Journal|June 1, 1993
Comparative kinetic study between native and chemically modified Cu,Zn superoxide dismutasesE Argese, R Girotto, E F Orsega
Chemosphere|April 2, 1999
Quantitative structure-activity relationships for the toxicity of chlorophenols to mammalian submitochondrial particlesE Argese, C Bettiol, G Giurin, et al.
Chemosphere|May 10, 2002
Heavy metal contamination in the seaweeds of the Venice lagoonM Caliceti, E Argese, A Sfriso, et al.
Biochemistry|June 2, 1987
Electrostatic control of the rate-determining step of the copper, zinc superoxide dismutase catalytic reactionE Argese, P Viglino, G Rotilio, et al.
The Journal of Biological Chemistry|September 10, 1981
Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutaseD Cocco, L Calabrese, A Rigo, et al.
The Journal of Biological Chemistry|March 25, 1979
Nuclear magnetic relaxation of 19F as a novel assay method of superoxide dismutaseA Rigo, P Viglino, E Argese, et al.
Analytical Biochemistry|July 1, 1983
A rotating disk electrode for kinetic studies of superoxide dismutases: applicability in a wide pH range and for continuous monitoring of enzyme inactivationE Argese, B De Carli, E Orsega, et al.
European Biophysics Journal : EBJ|January 1, 1987
The active site of manganese-containing superoxide dismutase from Bacillus stearothermophilus studied by 1H and 19F magnetic relaxationP Viglino, E F Orsega, E Argese, et al.
Molecular and Cellular Biochemistry|January 1, 1983
A comparative study of bovine, porcine and yeast superoxide dismutasesF Marmocchi, E Argese, A Rigo, et al.
Environmental Toxicology and Chemistry|May 10, 2001
Assessment of chloroaniline toxicity by the submitochondrial particle assayE Argese, C Bettiol, F Agnoli, et al.
Pageof 2

Showing results (1-10 of 11) with videos related to

Sort By:
Pageof 2
The Biochemical Journal|June 1, 1993
Comparative kinetic study between native and chemically modified Cu,Zn superoxide dismutasesE Argese, R Girotto, E F Orsega
Chemosphere|April 2, 1999
Quantitative structure-activity relationships for the toxicity of chlorophenols to mammalian submitochondrial particlesE Argese, C Bettiol, G Giurin, et al.
Chemosphere|May 10, 2002
Heavy metal contamination in the seaweeds of the Venice lagoonM Caliceti, E Argese, A Sfriso, et al.
Biochemistry|June 2, 1987
Electrostatic control of the rate-determining step of the copper, zinc superoxide dismutase catalytic reactionE Argese, P Viglino, G Rotilio, et al.
The Journal of Biological Chemistry|September 10, 1981
Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutaseD Cocco, L Calabrese, A Rigo, et al.
The Journal of Biological Chemistry|March 25, 1979
Nuclear magnetic relaxation of 19F as a novel assay method of superoxide dismutaseA Rigo, P Viglino, E Argese, et al.
Analytical Biochemistry|July 1, 1983
A rotating disk electrode for kinetic studies of superoxide dismutases: applicability in a wide pH range and for continuous monitoring of enzyme inactivationE Argese, B De Carli, E Orsega, et al.
European Biophysics Journal : EBJ|January 1, 1987
The active site of manganese-containing superoxide dismutase from Bacillus stearothermophilus studied by 1H and 19F magnetic relaxationP Viglino, E F Orsega, E Argese, et al.
Molecular and Cellular Biochemistry|January 1, 1983
A comparative study of bovine, porcine and yeast superoxide dismutasesF Marmocchi, E Argese, A Rigo, et al.
Environmental Toxicology and Chemistry|May 10, 2001
Assessment of chloroaniline toxicity by the submitochondrial particle assayE Argese, C Bettiol, F Agnoli, et al.
Pageof 2