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T Keleti

Showing results (31-40 of 46) with videos related to

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Journal of Theoretical Biology|February 21, 1988
The control of cell metabolism for homogeneous vs. heterogeneous enzyme systemsG R Welch, T Keleti, B Vértessy
Acta Biologica Et Medica Germanica|January 1, 1973
Reappraisal of the kinetics, mechanism of action and thermodynamics of d-glyceraldehyde-3-phosphate dehydrogenase actionT Keleti, J Batke, T Q Tro
European Journal of Biochemistry|January 1, 1982
Kinetics of coupled reactions catalyzed by aspartate aminotransferase and glutamate dehydrogenaseC Salerno, J Ovádi, T Keleti, et al.
Archives of Biochemistry and Biophysics|March 1, 1979
Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenaseJ Ovádi, J Batke, F Bartha, et al.
European Journal of Biochemistry|December 30, 1987
A kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates. Rat liver L-threonine dehydratase has a single active site for threonine and serineT Keleti, R Leoncini, R Pagani, et al.
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1977
Mechanism of action of D-glyceraldehyde-3-phosphate dehydrogenaseM Feraudi, M Kohlmeier, W Glaser, et al.
Biochimica Et Biophysica Acta|January 19, 1989
Double inhibition of L-threonine dehydratase by aminothiolsR Leoncini, R Pagani, E Marinello, et al.
European Journal of Biochemistry|October 14, 1971
Functional non-identity of subunits and isolation of active dimers of D-glyceraldehyde-3-phosphate dehydrogenaseJ Ovãdi, M Telegdi, J Batke, et al.
European Journal of Biochemistry|October 16, 1978
Physico-chemical evidence for the interaction between aldolase and glyceraldehyde-3-phosphate dehydrogenaseJ Ovádi, C Salerno, T Keleti, et al.
Biochimica Et Biophysica Acta|May 12, 1972
Some thermodynamic data on D-glyceraldehyde-3-phosphate dehydrogenase action under optimal conditionsT Keleti, J Földi, S Erdei, et al.
Pageof 5

Showing results (31-40 of 46) with videos related to

Sort By:
Pageof 5
Journal of Theoretical Biology|February 21, 1988
The control of cell metabolism for homogeneous vs. heterogeneous enzyme systemsG R Welch, T Keleti, B Vértessy
Acta Biologica Et Medica Germanica|January 1, 1973
Reappraisal of the kinetics, mechanism of action and thermodynamics of d-glyceraldehyde-3-phosphate dehydrogenase actionT Keleti, J Batke, T Q Tro
European Journal of Biochemistry|January 1, 1982
Kinetics of coupled reactions catalyzed by aspartate aminotransferase and glutamate dehydrogenaseC Salerno, J Ovádi, T Keleti, et al.
Archives of Biochemistry and Biophysics|March 1, 1979
Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenaseJ Ovádi, J Batke, F Bartha, et al.
European Journal of Biochemistry|December 30, 1987
A kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates. Rat liver L-threonine dehydratase has a single active site for threonine and serineT Keleti, R Leoncini, R Pagani, et al.
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1977
Mechanism of action of D-glyceraldehyde-3-phosphate dehydrogenaseM Feraudi, M Kohlmeier, W Glaser, et al.
Biochimica Et Biophysica Acta|January 19, 1989
Double inhibition of L-threonine dehydratase by aminothiolsR Leoncini, R Pagani, E Marinello, et al.
European Journal of Biochemistry|October 14, 1971
Functional non-identity of subunits and isolation of active dimers of D-glyceraldehyde-3-phosphate dehydrogenaseJ Ovãdi, M Telegdi, J Batke, et al.
European Journal of Biochemistry|October 16, 1978
Physico-chemical evidence for the interaction between aldolase and glyceraldehyde-3-phosphate dehydrogenaseJ Ovádi, C Salerno, T Keleti, et al.
Biochimica Et Biophysica Acta|May 12, 1972
Some thermodynamic data on D-glyceraldehyde-3-phosphate dehydrogenase action under optimal conditionsT Keleti, J Földi, S Erdei, et al.
Pageof 5