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J Batke

Showing results (1-10 of 42) with videos related to

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FEBS Letters|July 17, 1989
Remarks on the supramolecular organization of the glycolytic system in vivoJ 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 fluorometerJ Batke
Journal of Theoretical Biology|September 7, 1991
Channelling by loose enzyme complexes in situ is likely, though physiological significance is open for speculationJ Batke
Journal of Theoretical Biology|February 1, 1972
Modelling of allosteric interactions in dissociable tetrameric isoenzyme systemsJ Batke
Trends in Biochemical Sciences|December 1, 1989
Channeling of glycolytic intermediates by temporary, stationary bi-enzyme complexes is probable in vivoJ Batke
Biochemical Pharmacology|August 17, 1993
Suicide inhibition of monoamine oxidases A and B by (-)-deprenyl. A computer-aided solution for determining inhibition specificityJ 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 measurementsP Tompa, J Batke
Journal of Biochemical and Biophysical Methods|April 1, 1986
Displacement analysis of binding inhomogeneities in crude extracts of receptorsJ 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 coupleM 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 dehydrogenaseM Vas, J Batke
Pageof 5

Showing results (1-10 of 42) with videos related to

Sort By:
Pageof 5
FEBS Letters|July 17, 1989
Remarks on the supramolecular organization of the glycolytic system in vivoJ 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 fluorometerJ Batke
Journal of Theoretical Biology|September 7, 1991
Channelling by loose enzyme complexes in situ is likely, though physiological significance is open for speculationJ Batke
Journal of Theoretical Biology|February 1, 1972
Modelling of allosteric interactions in dissociable tetrameric isoenzyme systemsJ Batke
Trends in Biochemical Sciences|December 1, 1989
Channeling of glycolytic intermediates by temporary, stationary bi-enzyme complexes is probable in vivoJ Batke
Biochemical Pharmacology|August 17, 1993
Suicide inhibition of monoamine oxidases A and B by (-)-deprenyl. A computer-aided solution for determining inhibition specificityJ 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 measurementsP Tompa, J Batke
Journal of Biochemical and Biophysical Methods|April 1, 1986
Displacement analysis of binding inhomogeneities in crude extracts of receptorsJ 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 coupleM 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 dehydrogenaseM Vas, J Batke
Pageof 5