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W Maret

Showing results (41-50 of 53) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|March 3, 1999
Inhibitory sites in enzymes: zinc removal and reactivation by thioneinW Maret, C Jacob, B L Vallee, et al.
Biochemistry|June 21, 1983
Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analogueW Maret, M Zeppezauer, J Sanders-Loehr, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 16, 2000
Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole moleculeL J Jiang, M Vasák, B L Vallee, et al.
FEBS Letters|December 21, 1981
Ligand binding to the blue copper center of horse liver alcohol dehydrogenaseW Maret, M Zeppezauer, A Desideri, et al.
Biochimica Et Biophysica Acta|March 16, 1983
An EPR study of the blue copper center in horse liver alcohol dehydrogenaseW Maret, M Zeppezauer, A Desideri, et al.
European Journal of Biochemistry|November 15, 1978
Agarose-bound horse-liver alcohol dehydrogenase. Dependence of molecular properties and activity on coupling conditionsH Schneider-Bernlöhr, H Dietrich, W Maret, et al.
European Biophysics Journal : EBJ|January 1, 1987
The influence of anions and inhibitors on the catalytic metal ion in Co(II)-substituted horse liver alcohol dehydrogenaseI Bertini, G Lanini, C Luchinat, et al.
Biochemistry|June 9, 1981
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ionsI Andersson, W Maret, M Zeppezauer, et al.
Biochemistry|June 9, 1981
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(II) and competition with zinc(II) and cadmium(II) ionsI Andersson, W Maret, M Zeppezauer, et al.
European Journal of Biochemistry|December 22, 1989
Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzymeC Karlsson, W Maret, D S Auld, et al.
Pageof 6

Showing results (41-50 of 53) with videos related to

Sort By:
Pageof 6
Proceedings of the National Academy of Sciences of the United States of America|March 3, 1999
Inhibitory sites in enzymes: zinc removal and reactivation by thioneinW Maret, C Jacob, B L Vallee, et al.
Biochemistry|June 21, 1983
Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analogueW Maret, M Zeppezauer, J Sanders-Loehr, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 16, 2000
Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole moleculeL J Jiang, M Vasák, B L Vallee, et al.
FEBS Letters|December 21, 1981
Ligand binding to the blue copper center of horse liver alcohol dehydrogenaseW Maret, M Zeppezauer, A Desideri, et al.
Biochimica Et Biophysica Acta|March 16, 1983
An EPR study of the blue copper center in horse liver alcohol dehydrogenaseW Maret, M Zeppezauer, A Desideri, et al.
European Journal of Biochemistry|November 15, 1978
Agarose-bound horse-liver alcohol dehydrogenase. Dependence of molecular properties and activity on coupling conditionsH Schneider-Bernlöhr, H Dietrich, W Maret, et al.
European Biophysics Journal : EBJ|January 1, 1987
The influence of anions and inhibitors on the catalytic metal ion in Co(II)-substituted horse liver alcohol dehydrogenaseI Bertini, G Lanini, C Luchinat, et al.
Biochemistry|June 9, 1981
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ionsI Andersson, W Maret, M Zeppezauer, et al.
Biochemistry|June 9, 1981
Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(II) and competition with zinc(II) and cadmium(II) ionsI Andersson, W Maret, M Zeppezauer, et al.
European Journal of Biochemistry|December 22, 1989
Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzymeC Karlsson, W Maret, D S Auld, et al.
Pageof 6