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FEBS Letters
|
July 17, 1989
Remarks on the supramolecular organization of the glycolytic system in vivo
J Batke
Analytical Biochemistry
|
March 15, 1982
Spectrofluorometric analysis of the dissociation of oligomeric macromolecules: correction for the absorption of exciting and emitted light in a side-bottom type fluorometer
J Batke
Journal of Theoretical Biology
|
September 7, 1991
Channelling by loose enzyme complexes in situ is likely, though physiological significance is open for speculation
J Batke
Journal of Theoretical Biology
|
February 1, 1972
Modelling of allosteric interactions in dissociable tetrameric isoenzyme systems
J Batke
Trends in Biochemical Sciences
|
December 1, 1989
Channeling of glycolytic intermediates by temporary, stationary bi-enzyme complexes is probable in vivo
J Batke
Biochemical Pharmacology
|
August 17, 1993
Suicide inhibition of monoamine oxidases A and B by (-)-deprenyl. A computer-aided solution for determining inhibition specificity
J Batke, J Gaál
Biochemistry International
|
January 1, 1990
Fructose-1,6-bisphosphate aldolase preferentially associates to glyceraldehyde-3-phosphate dehydrogenase in a mixture of cytosolic proteins as revealed by fluorescence energy transfer measurements
P Tompa, J Batke
Journal of Biochemical and Biophysical Methods
|
April 1, 1986
Displacement analysis of binding inhomogeneities in crude extracts of receptors
J Batke, J Gaál
European Journal of Biochemistry
|
August 17, 1990
Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme-enzyme interaction. The example of 3-phospho-D-glycerate kinase and glyceraldehyde-3-phosphate dehydrogenase couple
M Vas, J Batke
Biochimica Et Biophysica Acta
|
August 13, 1981
Evidence for absence of an interaction between purified 3-phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase
M Vas, J Batke
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of 5
Search research articles
Search
Showing results (1-10 of 42) with videos related to
Sort By:
Page
of 5
FEBS Letters
|
July 17, 1989
Remarks on the supramolecular organization of the glycolytic system in vivo
J Batke
Analytical Biochemistry
|
March 15, 1982
Spectrofluorometric analysis of the dissociation of oligomeric macromolecules: correction for the absorption of exciting and emitted light in a side-bottom type fluorometer
J Batke
Journal of Theoretical Biology
|
September 7, 1991
Channelling by loose enzyme complexes in situ is likely, though physiological significance is open for speculation
J Batke
Journal of Theoretical Biology
|
February 1, 1972
Modelling of allosteric interactions in dissociable tetrameric isoenzyme systems
J Batke
Trends in Biochemical Sciences
|
December 1, 1989
Channeling of glycolytic intermediates by temporary, stationary bi-enzyme complexes is probable in vivo
J Batke
Biochemical Pharmacology
|
August 17, 1993
Suicide inhibition of monoamine oxidases A and B by (-)-deprenyl. A computer-aided solution for determining inhibition specificity
J Batke, J Gaál
Biochemistry International
|
January 1, 1990
Fructose-1,6-bisphosphate aldolase preferentially associates to glyceraldehyde-3-phosphate dehydrogenase in a mixture of cytosolic proteins as revealed by fluorescence energy transfer measurements
P Tompa, J Batke
Journal of Biochemical and Biophysical Methods
|
April 1, 1986
Displacement analysis of binding inhomogeneities in crude extracts of receptors
J Batke, J Gaál
European Journal of Biochemistry
|
August 17, 1990
Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme-enzyme interaction. The example of 3-phospho-D-glycerate kinase and glyceraldehyde-3-phosphate dehydrogenase couple
M Vas, J Batke
Biochimica Et Biophysica Acta
|
August 13, 1981
Evidence for absence of an interaction between purified 3-phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase
M Vas, J Batke
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of 5