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  • 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
RESUMO

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

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Acetilcolinesterase, Type V-S, lyophilized powder, ≥1,000 units/mg protein
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Acetylthiocholine chloride, ≥99% (TLC), powder