New methods for the study of complex enzyme kinetics illustrated by analysis of the wavy curves of v versus (S) and non-linear double-reciprocal plots for human-placental 15-hydroxyprostaglandin dehydrogenase.

  title={New methods for the study of complex enzyme kinetics illustrated by analysis of the wavy curves of v versus (S) and non-linear double-reciprocal plots for human-placental 15-hydroxyprostaglandin dehydrogenase.},
  author={William G. Bardsley and M. James C. Crabbe},
  journal={European journal of biochemistry},
  volume={68 2},
A new method for discovering the minimum degree of rate equations using only the experimental graphs and a straight-edge (transparent ruler) is presented. This method is then illustrated by an analysis of the wavy v vs [S] curves and non-linear double-reciprocal plots reproducibly given by NAD-dependent 15-hydroxyprostaglandin dehydrogenase for which a new improved purification is described. It is shown by this analysis that the enzyme has a complex mechanism involving cooperatively linked… 
17 Citations
Does any enzyme follow the Michaelis—Menten equation?
The assumption that most enzymes follow the Michaelis—Menten equation can not be supported by an appeal to the literature, and the minimum degree of the rate equation is determined.
Steady-state kinetics of smooth muscle myosin.
  • M. Malik
  • Biology, Chemistry
  • 1978
The kinetic properties of purified smooth muscle myosin, free of actin, have been examined and analysis of the steady-state kinetic data revealed an intermediary plateau region on the substrate saturation curves, suggesting at least four substrate binding sites.
Modulation of the substrate binding sites of platelet myosin by actin.
  • M. Malik
  • Biology
    Archives of biochemistry and biophysics
  • 1979
Kinetic and binding properties of the oxoglutarate translocator of rat-heart mitochondria.
The kinetic study of the oxoglutarateout/malatein exchange through the inner mitochondrial membrane of rat-heart mitochondria has been compelted and extended to higher external-oxoglutarate and to
Thermodynamics of information transfer between subunits in oligomeric enzymes and kinetic cooperativity. 2. Thermodynamics of kinetic cooperativity.
The principles of structural kinetics allow one to define the thermodynamic conditions that are sufficient to generate a certain type of kinetic behavior and the boundaries between the necessary conditions and the lack of these conditions are determined.


The quantitative analysis of ligand binding and initial-rate data for allosteric and other complex enzyme mechanisms.
  • W. Bardsley
  • Materials Science
    The Biochemical journal
  • 1976
1. The eight methods for plotting enzyme kinetic data are classified and analysed, and it is shown how, in each case, it is only possible to obtain quantitative data on the coefficients of the
[15-Hydroxyprostaglandin dehydrogenase from human placenta, II. Steady state kinetics and influence of prostaglandin F2alpha analogues (author's transl)].
The initial rate and inhibition patterns obtained indicate that the reaction follows kinetically an ordered Bi Bi mechanism and is likely to have biological significance.
Steady-state kinetics of lactoperoxidase with ABTS as chromogen.
Kinetic formulations for enzymic reactions involving two substrates.
  • J. Wong, C. Hanes
  • Biology, Computer Science
    Canadian journal of biochemistry and physiology
  • 1962
An analysis has been made of the structure of steady-state rate equations, which permits the establishment of direct relationships between specified features of mechanism and of rate behavior and opens up the possibility of a featurewise approach for the progressive elucidation of complex enzyme mechanisms.
Sigmoid curves, non-linear double-reciprocal plots and allosterism.
The theory of plane curves was applied to the graphical methods used in enzyme kinetics and a mathematical analysis of the possible graph shapes is given and it is suggested that the usual methods of interpreting steady-state kinetic data are often based on over-restrictive assumptions which prevent maximum utilization of the available data.
The steady-state kinetics of peroxidase with 2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen.
An interpretation of the results is given which requires some extension of the classical peroxidase mechanism, and a study of the steady-state kinetics over a whole range of substrate concentrations is reported.