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Biochemistry|November 28, 1989
Evolutionary optimization of the catalytic effectiveness of an enzymeJ J Burbaum, R T Raines, W J Albery, et al.Biochemistry|December 14, 1976
Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in productS J Fletcher, J M Herlihy, W J Albery, et al.Biochemistry|May 6, 1986
Energetics of proline racemase: fractionation factors for the essential catalytic groups in the enzyme-substrate complexesJ G Belasco, T W Bruice, W J Albery, et al.Biochemistry|May 6, 1986
Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic stepsL M Fisher, J G Belasco, T W Bruice, et al.Biochemistry|May 6, 1986
Energetics of proline racemase: rates, fractionation factors, and buffer catalysis in the oversaturated region. Nature of the interconversion of the two forms of free enzymeJ G Belasco, T W Bruice, L M Fisher, et al.The Journal of Pharmacy and Pharmacology|March 1, 1979
Percutaneous absorption: in vivo experimentsW J Albery, J HadgraftThe Journal of Pharmacy and Pharmacology|March 1, 1979
Percutaneous absorption: theoretical descriptionW J Albery, J HadgraftThe Journal of Pharmacy and Pharmacology|February 1, 1979
Percutaneous absorption: interfacial transfer kineticsW J Albery, J HadgraftPageof 16