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T Keleti

Showing results (1-10 of 46) with videos related to

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The Biochemical Journal|April 1, 1982
A novel parameter estimation from the linearized Michaelis-Menten equation at low substrate concentrationsT Keleti
The Biochemical Journal|January 1, 1983
Errors in the evaluation of Arrhenius and van't Hoff plotsT Keleti
Analytical Biochemistry|January 1, 1986
Determination of Michaelis-Menten parameters from initial velocity measurements using unstable substrateT Keleti
FEBS Letters|April 16, 1970
The excimer fluorescence of tryptophan, tyrosine and d-glyceraldehyde-3-phosphate dehydrogenaseT Keleti
Journal of Theoretical Biology|March 1, 1971
Simple mechanisms for the modification of homotetrameric proteinsT Keleti
FEBS Letters|December 15, 1972
New method to differentiate between some mechanisms of action of enzymes with three substratesT Keleti
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1985
Stability, heat stability and heat sensitivity of proteins: thermodynamic considerationsT Keleti
FEBS Letters|November 10, 1986
Two rules of enzyme kinetics for reversible Michaelis-Menten mechanismsT Keleti
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1972
Heat denaturation of D-glyceraldehyde-3-phosphate dehydrogenase holoenzymeT Keleti, M Szegvári
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1975
Sigmoidal substrate saturation curves in Michaelis-Menten mechanism as an artefactE Fischer, T Keleti
Pageof 5

Showing results (1-10 of 46) with videos related to

Sort By:
Pageof 5
The Biochemical Journal|April 1, 1982
A novel parameter estimation from the linearized Michaelis-Menten equation at low substrate concentrationsT Keleti
The Biochemical Journal|January 1, 1983
Errors in the evaluation of Arrhenius and van't Hoff plotsT Keleti
Analytical Biochemistry|January 1, 1986
Determination of Michaelis-Menten parameters from initial velocity measurements using unstable substrateT Keleti
FEBS Letters|April 16, 1970
The excimer fluorescence of tryptophan, tyrosine and d-glyceraldehyde-3-phosphate dehydrogenaseT Keleti
Journal of Theoretical Biology|March 1, 1971
Simple mechanisms for the modification of homotetrameric proteinsT Keleti
FEBS Letters|December 15, 1972
New method to differentiate between some mechanisms of action of enzymes with three substratesT Keleti
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1985
Stability, heat stability and heat sensitivity of proteins: thermodynamic considerationsT Keleti
FEBS Letters|November 10, 1986
Two rules of enzyme kinetics for reversible Michaelis-Menten mechanismsT Keleti
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1972
Heat denaturation of D-glyceraldehyde-3-phosphate dehydrogenase holoenzymeT Keleti, M Szegvári
Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae|January 1, 1975
Sigmoidal substrate saturation curves in Michaelis-Menten mechanism as an artefactE Fischer, T Keleti
Pageof 5