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Biochemistry|December 14, 1976
Free-energy profile of the reaction catalyzed by triosephosphate isomeraseW J Albery, J R KnowlesBiochemistry|December 14, 1976
Deuterium and tritium exchange in enzyme kineticsW J Albery, J R KnowlesJournal of Theoretical Biology|January 21, 1987
Energetics of enzyme catalysis. I. Isotopic experiments, enzyme interconversion, and oversaturationW J Albery, J R KnowlesJournal of Theoretical Biology|January 21, 1987
Energetics of enzyme catalysis. II. Oversaturation, case diagrams, reversible and irreversible behaviourW J Albery, J R KnowlesBiochemistry|May 6, 1986
Energetics of proline racemase: tracer perturbation experiments using [14C]proline that measure the interconversion rate of the two forms of free enzymeL M Fisher, W J Albery, J R KnowlesBiochemistry|December 14, 1976
Energetics of triosephosphate isomerase: the nature of the proton transfer between the catalytic base and solvent waterL M Fisher, W J Albery, J R KnowlesBiochemistry|May 6, 1986
Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated, and oversaturated regimesL M Fisher, W J Albery, J R KnowlesBiochemistry|December 14, 1976
Energetics of triosephosphate isomerase: deuterium isotope effects in the enzyme-catalyzed reactionP F Leadlay, W J Albery, J R KnowlesBiochemistry|May 6, 1986
Energetics of proline racemase: double fractionation experiment, a test for concertedness and for transition-state dominanceJ G Belasco, W J Albery, J R KnowlesBiochemistry|December 14, 1976
Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in productS G Maister, C P Pett, W J Albery, et al.Pageof 16