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PMID: 1218081 Published · ppublish English Journal Article

Factorization of the Michaelis functions.

The Biochemical journal ·Vol. 151 ·No. 2 ·1975-11-00 ·Pages 271-4

Dixon HB

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.

MeSH Terms
Binding Sites Enzymes/metabolism Kinetics Ligands
Chemicals
Enzymes Ligands
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Dixon H B
References (5)
5 references, click to expand
  1. Shapes of curves of pH-dependence of reactions.
    Biochem J. 1973 Jan;131(1):149-54 PMID: 4722033
  2. The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart.
    Biochem J. 1974 Aug;141(2):401-6 PMID: 4455213
  3. pH-controlled hydrogen-bonding.
    Biochem J. 1974 Dec;143(3):775-7 PMID: 4462756
  4. Negatively co-operative ligand binding.
    Biochem J. 1973 Aug;133(4):837-42 PMID: 4748836
  5. Curves of ligand binding. The use of hyperbolic functions for expressing titration curves.
    Biochem J. 1974 Mar;137(3):443-7 PMID: 4420319
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1975-11-00
Pages
271-4
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1172356
Subset
IM
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