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.
MeSH terms
-
Acetyl Coenzyme A / metabolism
-
Animals
-
Binding, Competitive
-
Chloramphenicol / metabolism
-
Chloramphenicol O-Acetyltransferase / antagonists & inhibitors*
-
Chloramphenicol O-Acetyltransferase / genetics
-
Deoxycholic Acid / pharmacology
-
Detergents / pharmacology*
-
Dose-Response Relationship, Drug
-
Glucosides / pharmacology
-
HeLa Cells
-
Humans
-
Kinetics
-
Models, Biological
-
Octoxynol / pharmacology
-
Polyethylene Glycols / pharmacology
-
Polysorbates / pharmacology
-
Sodium Dodecyl Sulfate / pharmacology
-
Transfection
Substances
-
Detergents
-
Glucosides
-
Polysorbates
-
Deoxycholic Acid
-
octyl-beta-D-glucoside
-
Sodium Dodecyl Sulfate
-
Polyethylene Glycols
-
dodecyl glucoside
-
Chloramphenicol
-
Acetyl Coenzyme A
-
Octoxynol
-
Nonidet P-40
-
Chloramphenicol O-Acetyltransferase