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Search Publications by: Robert N Goldberg (Assoc)

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Displaying 51 - 75 of 91

Thermodynamics of Enzyme-Catalyzed Reactions: Part 6. 1999 Update

April 1, 1999
Author(s)
Robert N. Goldberg
This review serves to update previously published evaluations of equilibrium constants and enthalpy changes for enzyme-catalyzed reactions. For each reaction the following information is given: the reference for the data; the reaction studied; the name of

A Thermodynamic Investigation of Some Reactions Involving Prephenic Acid

February 1, 1999
Author(s)
N Kishore, Marcia J. Holden, Yadu D. Tewari, Robert N. Goldberg
Calorimetric enthalpies of reaction have been measured for the following enzyme-catalyzed reactions at the temperature 298.15 Kprephenate(aq) = phenylpyruvate(aq) + H 20(l) + carbon dioxide(aq), prephenate(aq) + NAD ox(aq) = 4-hydroxyphenylpyruvate(aq) +

A Thermodynamic Investigation of Reactions Catalyzed by Tryptophan Synthase

July 27, 1998
Author(s)
N Kishore, Yadu D. Tewari, D Akers, Robert N. Goldberg, E. W. Miles
Microcalorimetry and high-performance liquid chromatography have been used to conduct a thermodynamic investigation of the following reactions catalyzed by the tryptophan synthase [alpha] 2[Beta] 2 complex (EC 4.2.1.20) and its subunits:indole(aq) + L

An Equilibrium and Calorimetric Study of Some Transamination Reactions

June 1, 1998
Author(s)
Yadu D. Tewari, N Kishore, Robert N. Goldberg, T N. Luong
Apparent equilibrium constants and calorimetric enthalpies of reaction have been measured for the following enzyme-catalyzed biochemical reactions at the temperature 298.15 k:l-alanine(aq) + 2-oxoglutarate(aq) = pyruvate(aq) + L-glutamate(aq); L-tyrosine