๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

A steady-state kinetic method for the verification of the rapid-equilibrium assumption in allosteric enzymes

โœ Scribed by Marina M. Symcox; Gregory D. Reinhart


Book ID
107719068
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
606 KB
Volume
206
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


A general solution for the steady-state
โœ D.C. Rees ๐Ÿ“‚ Article ๐Ÿ“… 1984 ๐Ÿ› Springer ๐ŸŒ English โš– 280 KB

A power series solution is presented which describes the steady-state concentration profiles for substrate and product molecules in immobilized enzyme systems. Diffusional effects and product inhibition are incorporated into this model. The kinetic consequences of diffusion limitation and product in

On the Relationship Between the Hill Coe
โœ Amnon Horovitz; Ofer Yifrach ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› Springer ๐ŸŒ English โš– 61 KB

A frequently used measure for the extent of cooperativity in ligand binding by allosteric proteins is the Hill coefficient. Hill coefficients can be measured for steady-state kinetic data and also for transient kinetic data. Here, the relationship between the two types of Hill coefficients is analys

An on-line method for the collection and
โœ Charles Walter; Heidi Eberspaecher; J. Patrick Hughes ๐Ÿ“‚ Article ๐Ÿ“… 1975 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 757 KB

A special mixing device for initiating enzyme-catalyzed reactions is used to rapidly achieve an unperturbed quasi-steady state. An on-line computer is employed to sample the initial conditions, the mixing time, and concentrations that change as a function of time during this quasi-steady state phase