Lu J, Jiang C
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY.
Biochem Biophys Res Commun. 1993 Oct 15;196(1):12-7. doi: 10.1006/bbrc.1993.2209.
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.
动力学分析表明,非离子去污剂Triton X-100和Nonidet P-40对氯霉素乙酰转移酶的抑制作用分别通过与底物氯霉素和乙酰辅酶A的竞争性和非竞争性机制发挥。与不像Triton X-100和Nonidet P-40那样含有芳香部分的非离子去污剂相比,表明这两种去污剂中的芳香基团可能与氯霉素竞争结合氯霉素乙酰转移酶中的疏水活性位点。