Literature DB >> 889566

An evaluation of ways of using equilibrium dialysis to quantify the binding of ligand to macromolecule.

I A Nimmo, G L Atkins, R C Strange, I W Percy-Robb.   

Abstract

1. The effect of systematic error (loss of ligand, complex or macromolecule) on three of the experimental designs by which equilibrium dialysis may be used to quantify the interaction of ligand and macromolecule is examined theoretically, and the design that is least sensitive to systematic error is identified. 2. Thirteen methods for fitting the binding isotherm to experimental data are compared by using them to analyse simulated data containing random error, and the most reliable method is identified.

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Year:  1977        PMID: 889566      PMCID: PMC1164874          DOI: 10.1042/bj1650107

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  9 in total

1.  A comparison of seven methods for fitting the Michaelis-Menten equation.

Authors:  G L Atkins; I A Nimmo
Journal:  Biochem J       Date:  1975-09       Impact factor: 3.857

2.  Statistical estimations in enzyme kinetics.

Authors:  G N WILKINSON
Journal:  Biochem J       Date:  1961-08       Impact factor: 3.857

3.  A pitfall in the interpretation of data on ligand-protein interaction.

Authors:  S Swillens; J E Dumont
Journal:  Biochem J       Date:  1975-09       Impact factor: 3.857

4.  Methods for fitting equations with two or more non-linear parameters.

Authors:  I A Nimmo; G L Atkins
Journal:  Biochem J       Date:  1976-08-01       Impact factor: 3.857

5.  Equilibrium-dialysis studies of the interaction between cholic acid and 100000g-supernatant preparations from the rat liver.

Authors:  R C Strange; I A Nimmo; I W Percy-Robb
Journal:  Biochem J       Date:  1976-05-15       Impact factor: 3.857

6.  A new method for determining the Michaelis constant.

Authors:  F M De Merino
Journal:  Biochem J       Date:  1974-10       Impact factor: 3.857

7.  The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters.

Authors:  R Eisenthal; A Cornish-Bowden
Journal:  Biochem J       Date:  1974-06       Impact factor: 3.857

8.  "Best values" of Michaelis-Menten kinetic constants from experimental data.

Authors:  S R Cohen
Journal:  Anal Biochem       Date:  1968-03       Impact factor: 3.365

9.  Binding of bile acids by 100 000g supernatants from rat liver.

Authors:  R C Strange; I A Nimmo; I W Percy-Robb
Journal:  Biochem J       Date:  1977-03-15       Impact factor: 3.857

  9 in total
  3 in total

1.  Binding of NAD+ by cholera toxin.

Authors:  T S Galloway; S van Heyningen
Journal:  Biochem J       Date:  1987-05-15       Impact factor: 3.857

2.  Treatment with isoproterenol of bupivacaine toxicity.

Authors:  P Lacombe; G Blaise; F Plante; C Hollmann
Journal:  Can J Anaesth       Date:  1990-05       Impact factor: 5.063

3.  Ultrafiltration vs equilibrium dialysis for determination of free fraction.

Authors:  W F Bowers; S Fulton; J Thompson
Journal:  Clin Pharmacokinet       Date:  1984-01       Impact factor: 6.447

  3 in total

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