Literature DB >> 1218081

Factorization of the Michaelis functions.

H B Dixon.   

Abstract

Each Michaelis function that expresses the concentration of one of the species AL2, AL and A in terms of the concentration of free ligand (or its logarithm) is the product of two functions each of which represents the degree of ligation or de-ligation of a single site. These hypothetical sites have pK values of pK (SEE ARTICLE) where pK and alpha are defined by writing the two molecular pK values as pK +/- log2alpha. The factors are thus real if alpha larger than or equal to 1, i.e. if the binding of L by A is not positively co-operative. The dependence of [AL] on 1n[L] is compared with relations that represent other ligand-dependent equilibria.

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Year:  1975        PMID: 1218081      PMCID: PMC1172356          DOI: 10.1042/bj1510271

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


  5 in total

1.  Curves of ligand binding. The use of hyperbolic functions for expressing titration curves.

Authors:  H B Dixon
Journal:  Biochem J       Date:  1974-03       Impact factor: 3.857

2.  pH-controlled hydrogen-bonding.

Authors:  J L Wood
Journal:  Biochem J       Date:  1974-12       Impact factor: 3.857

3.  Shapes of curves of pH-dependence of reactions.

Authors:  H B Dixon
Journal:  Biochem J       Date:  1973-01       Impact factor: 3.857

4.  Negatively co-operative ligand binding.

Authors:  H B Dixon; K F Tipton
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

5.  The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart.

Authors:  R John; R Jones
Journal:  Biochem J       Date:  1974-08       Impact factor: 3.857

  5 in total
  6 in total

1.  PH-dependence of the steady-state rate of a two-step enzymic reaction.

Authors:  K Brocklehurst; H B Dixon
Journal:  Biochem J       Date:  1976-04-01       Impact factor: 3.857

2.  The origin of multiply sigmoid curves of pH-dependence. The partitioning of groups among titration pK values.

Authors:  H B Dixon; S D Clarke; G A Smith; T K Carne
Journal:  Biochem J       Date:  1991-08-15       Impact factor: 3.857

3.  The unreliability of estimates of group dissociation constants.

Authors:  H B Dixon
Journal:  Biochem J       Date:  1976-03-01       Impact factor: 3.857

4.  pH-activity curves for enzyme-catalysed reactions in which the hydron is a product or reactant.

Authors:  H B Dixon; K Brocklehurst; K F Tipton
Journal:  Biochem J       Date:  1987-12-01       Impact factor: 3.857

5.  Derivation of molecular pK values from pH-dependences.

Authors:  H B Dixon
Journal:  Biochem J       Date:  1979-01-01       Impact factor: 3.857

6.  Relations between the dissociation constants of dibasic acids.

Authors:  H B Dixon
Journal:  Biochem J       Date:  1988-08-01       Impact factor: 3.857

  6 in total

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