A Note on the Kinetics of Enzyme Action

Briggs, G. E., & Haldane, J. B. S. (1925). A Note on the Kinetics of Enzyme Action. Biochemical Journal, 19(2), 338-339.

Type

Journal article

Intellectual base

Primary research

Year

1925

DOI

10.1042/bj0190338

Link

https://doi.org/10.1042/bj0190338

Cited from

chemistry_materials, pharmacology_toxicology

Cited by

3 citations across 3 artifacts.

Each citation links to the sentence it supports in the citing article.

Primes

• Reaction Intermediate
  • Under the steady-state approximation, the standing population of the intermediate is set by the formation/consumption ratio: \([ES] = \frac{[E][S]}{(k_{-1}+k_2)/k_1} = \frac{[E][S]}{K_M}\).

    This sourceIntroduces the steady-state approximation giving [ES] from the formation/consumption ratio and V_max at saturation.

• Receptor Saturation
  • Drawing on the steady-state enzyme-kinetic foundation Briggs and Haldane (1925) established,

Domain-specific

• Michaelis–Menten Kinetics
  • The latter does not require rapid binding equilibrium.

Verification

This reference passed the adversarial substantiation pipeline: it was checked to exist and to support the claim it is attached to. See how references were verified.

Registry ID ref:b0f6437fa164 · see in the full table