Literature DB >> 475775

The determination of binding parameters when the total and free substrate concentrations are not approximately equal.

N Gains.   

Abstract

By using a standard graphical method values of Km and V may be found that are independent of the conditions and assumptions that the total substrate concentration approximates to its free concentration and that Km is much larger than the enzyme concentration. The procedure is also applicable to the determination of equilibrium binding parameters of a ligand to a macromolecule.

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Year:  1979        PMID： 475775      PMCID： PMC1186679          DOI： 10.1042/bj1790697

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


  9 in total

1.  GRAPHICAL DETERMINATION OF EQUILIBRIUM CONSTANTS.

Authors:  M DIXON
Journal:  Biochem J       Date:  1965-03       Impact factor: 3.857

2.  Non-inverted versus inverted plots in enzyme kinetics.

Authors:  B H HOFSTEE
Journal:  Nature       Date:  1959-10-24       Impact factor: 49.962

3.  The partial purification and properties of animal and plant hydantoinases.

Authors:  G S EADIE; F BERNHEIM; M L C BERNHEIM
Journal:  J Biol Chem       Date:  1949-12       Impact factor: 5.157

4.  Determination of dissociation and Michaelis constants at near-equal enzyme-substrate concentrations.

Authors:  G D Smith; R Eisenthal; R Harrison
Journal:  Anal Biochem       Date:  1977-05-01       Impact factor: 3.365

5.  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

6.  The graphical determination of K m and K i .

Authors:  M Dixon
Journal:  Biochem J       Date:  1972-08       Impact factor: 3.857

7.  A more general definition of Km [proceedings].

Authors:  J R Griffiths
Journal:  Biochem Soc Trans       Date:  1978       Impact factor: 5.407

8.  Steady-state enzyme kinetics in mutual depletion systems.

Authors:  J R Griffiths
Journal:  Biochem Soc Trans       Date:  1979-04       Impact factor: 5.407

9.  A modified graphical method for determination of equilibrium constants.

Authors:  T A Kilroe-Smith
Journal:  Biochem J       Date:  1966-08       Impact factor: 3.857
  9 in total
  2 in total

1.  The error in the Michaelis-Menten equation when substrate depletion by binding to the enzyme is not taken into account.

Authors:  K P Heirwegh; M Vermeir
Journal:  Biochem J       Date:  1992-04-15       Impact factor: 3.857

2.  A method for determining kinetic parameters at high enzyme concentrations.

Authors:  C J Halfman; F Marcus
Journal:  Biochem J       Date:  1982-04-01       Impact factor: 3.857
  2 in total

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