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T KELETI

Showing results (11-20 of 24) with videos related to

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Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1983
Homologous partial sequences in dehydrogenasesG Mátrai, F Darvas, T Keleti
Archives of Biochemistry and Biophysics|November 15, 1986
Microenvironment of the enzyme-bound NADH is different in lobster and pig muscle glyceraldehyde-3-phosphate dehydrogenase microcrystalsB Vértessy, M Vas, T Keleti
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1979
pH and temperature dependence of the double inhibition of D-glyceraldehyde-3-phosphate dehydrogenase by ATP and quinaldateL V Lien, H Koubakouenda, T Keleti
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 Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1979
Double inhibition of D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenaseL V Lien, G Ecsedi, T Keleti
Journal of Theoretical Biology|November 8, 1988
The perfection of substrate-channelling in interacting enzyme systems: energetics and evolutionT Keleti, B Vértessy, G R Welch
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.
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.
Biochimica Et Biophysica Acta|January 19, 1989
Double inhibition of L-threonine dehydratase by aminothiolsR Leoncini, R Pagani, E Marinello, et al.
Pageof 3

Showing results (11-20 of 24) with videos related to

Sort By:
Pageof 3
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1983
Homologous partial sequences in dehydrogenasesG Mátrai, F Darvas, T Keleti
Archives of Biochemistry and Biophysics|November 15, 1986
Microenvironment of the enzyme-bound NADH is different in lobster and pig muscle glyceraldehyde-3-phosphate dehydrogenase microcrystalsB Vértessy, M Vas, T Keleti
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1979
pH and temperature dependence of the double inhibition of D-glyceraldehyde-3-phosphate dehydrogenase by ATP and quinaldateL V Lien, H Koubakouenda, T Keleti
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 Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1979
Double inhibition of D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenaseL V Lien, G Ecsedi, T Keleti
Journal of Theoretical Biology|November 8, 1988
The perfection of substrate-channelling in interacting enzyme systems: energetics and evolutionT Keleti, B Vértessy, G R Welch
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.
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.
Biochimica Et Biophysica Acta|January 19, 1989
Double inhibition of L-threonine dehydratase by aminothiolsR Leoncini, R Pagani, E Marinello, et al.
Pageof 3