On the use of the experimentally determined enzyme inhibition constant as a measure of absolute binding affinity.

On the use of the experimentally determined enzyme inhibition constant as a measure of absolute binding affinity.

Biochemical and biophysical research communications (2017-06-03)

Fouad H Darras, Yuan-Ping Pang

RESUMEN

Defined as a state function representing an inhibitor's absolute affinity for its target enzyme, the experimentally determined enzyme inhibition constant (K

MATERIALES

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Descripción del producto

C2888

Sigma-Aldrich

Acetilcolinesterasa from Electrophorus electricus (electric eel), Type V-S, lyophilized powder, ≥1,000 units/mg protein

A5626

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Acetylthiocholine chloride, ≥99% (TLC), powder