INHIBITION-KINETICS OF CHLORAMPHENICOL ACETYLTRANSFERASE BY SELECTED DETERGENTS

被引:1
|
作者
LU, JX [1 ]
JIANG, C [1 ]
机构
[1] CORNELL UNIV,BIOCHEM MOLEC & CELL BIOL SECT,ITHACA,NY 14853
关键词
D O I
10.1006/bbrc.1993.2209
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. © 1993 Academic Press. All rights reserved.
引用
收藏
页码:12 / 17
页数:6
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