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Buffers of constant ionic strength for studying pH-dependent processes.
Publisher Summary This chapter outlines the procedures for calculating (a) the practical pKa values that apply to the buffer components under the chosen experimental conditions and (b) the ionicExpand
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Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors.
  • J. F. Morrison
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 19 August 1969
Abstract A theoretical kinetic study has been undertaken to determine the kinetic characteristics of enzymic reactions that are reversibly inhibited by a substrate analogue at concentrationsExpand
  • 595
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The kinetics of reversible tight-binding inhibition.
  • 158
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The activation of aconitase by ferrous ions and reducing agents.
  • J. F. Morrison
  • Chemistry, Medicine
  • The Biochemical journal
  • 1 December 1954
  • 81
  • 7
Mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrate.
The variations with pH of the kinetic parameters and primary deuterium isotope effects for the reaction of NADPH with dihydrofolate reductase from Escherichia coli have been determined. The aims ofExpand
  • 58
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The mechanism of the reaction catalysed by adenosine triphosphate-creatine phosphotransferase.
1. The forward and reverse reactions catalysed by ATP-creatine phosphotransferase have been studied kinetically at pH8.0 in the presence and absence of products, under conditions in which the freeExpand
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Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli.
The kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli has been investigated by using progress curve, initial velocity, product inhibition, and dead-endExpand
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Mechanism of inhibition of dihydrofolate reductases from bacterial and vertebrate sources by various classes of folate analogues.
Different classes of folate analogues have been examined with respect to the mechanism of their inhibition of dihydrofolate reductases from Escherichia coli and chicken liver. In addition, the degreeExpand
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The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli.
A simple and convenient procedure is described for the isolation in good yield of two amino-transferases from various strains of Escherichia coli. On the basis of their substrate specificities one ofExpand
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Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate.
The prephenate dehydrogenase activity of the bifunctional enzyme chorismate mutase-prephenate dehydrogenase from Escherichia coli catalyzes the oxidative decarboxylation of both prephenate andExpand
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