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-4O suggests that the aromatic groups in these two detergents may compete with chloramphenicol for binding to the hydrophobic, active site in the chloramphenicol acetyltransferase.
|Number of pages
|Biochemical and Biophysical Research Communications
|Published - Oct 15 1993
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology