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Merck

Inhibition kinetics of chloramphenicol acetyltransferase by selected detergents.

Biochemical and biophysical research communications (1993-10-15)
J Lu, C Jiang
ABSTRACT

Kinetic analyses indicate that the inhibitory effects of the nonionic detergents Triton X-100 and Nonidet P-40 on chloramphenicol acetyltransferase are exerted by a competitive and a non-competitive mechanism with respect to the substrates chloramphenicol and acetyl-CoA, respectively. Comparison with nonionic detergents without an aromatic moiety like that present in Triton X-100 and Nonidet P-40 suggests that the aromatic groups in these two detergents may compete with chloramphenicol for binding to the hydrophobic, active site in the chloramphenicol acetyltransferase.

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Sigma-Aldrich
n-Dodecyl β-D-glucopyranoside, ≥98% (GC)