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J Südi

Showing results (1-10 of 15) with videos related to

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Die Naturwissenschaften|December 12, 1997
How to derive steady-state rate laws for enzyme-catalyzed reactions from macroscopic probabilitiesJ Südi
The Biochemical Journal|February 1, 1976
Chiral recognition of prochiral centres and general acid-base catalysis. Necessarily interrelated manifestations of active-site structureJ Südi
Physiological Chemistry and Physics|January 1, 1976
The role of product release in enzyme catalysisJ Südi
Mathematical Biosciences|November 1, 1996
How to derive flux control coefficients from the rate equations of classical enzyme kineticsJ Südi
Biochimica Et Biophysica Acta|August 15, 1970
Kinetics of the protection of lactate dehydrogenase by substrates against heat inactivationJ Südi
Biochimica Et Biophysica Acta|November 14, 1997
Control analysis of enzyme mechanisms in terms of the classical steady-state descriptionJ Südi
The Biochemical Journal|April 1, 1974
Macroscopic rate constants involved in the formation and interconversion of the two central enzyme--substrate complexes of the lactate dehydrogenase turnoverJ Südi
The Biochemical Journal|May 15, 1992
Kinetic barriers under steady-state conditionsJ Südi
The Biochemical Journal|May 15, 1991
How to draw kinetic barrier diagrams for enzyme-catalysed reactionsJ Südi
The Biochemical Journal|April 1, 1974
The lactate dehydrogenase--reduced nicotinamide--adenine dinucleotide--pyruvate complex. Kinetics of pyruvate binding and quenching of coeznyme fluorescenceJ Südi
Pageof 2

Showing results (1-10 of 15) with videos related to

Sort By:
Pageof 2
Die Naturwissenschaften|December 12, 1997
How to derive steady-state rate laws for enzyme-catalyzed reactions from macroscopic probabilitiesJ Südi
The Biochemical Journal|February 1, 1976
Chiral recognition of prochiral centres and general acid-base catalysis. Necessarily interrelated manifestations of active-site structureJ Südi
Physiological Chemistry and Physics|January 1, 1976
The role of product release in enzyme catalysisJ Südi
Mathematical Biosciences|November 1, 1996
How to derive flux control coefficients from the rate equations of classical enzyme kineticsJ Südi
Biochimica Et Biophysica Acta|August 15, 1970
Kinetics of the protection of lactate dehydrogenase by substrates against heat inactivationJ Südi
Biochimica Et Biophysica Acta|November 14, 1997
Control analysis of enzyme mechanisms in terms of the classical steady-state descriptionJ Südi
The Biochemical Journal|April 1, 1974
Macroscopic rate constants involved in the formation and interconversion of the two central enzyme--substrate complexes of the lactate dehydrogenase turnoverJ Südi
The Biochemical Journal|May 15, 1992
Kinetic barriers under steady-state conditionsJ Südi
The Biochemical Journal|May 15, 1991
How to draw kinetic barrier diagrams for enzyme-catalysed reactionsJ Südi
The Biochemical Journal|April 1, 1974
The lactate dehydrogenase--reduced nicotinamide--adenine dinucleotide--pyruvate complex. Kinetics of pyruvate binding and quenching of coeznyme fluorescenceJ Südi
Pageof 2