J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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Journal of Lipid Research, Vol. 14, 459-465, July 1973
Copyright © 1973 by Lipid Research, Inc.

Inhibition of palmitoyl CoA deacylase by chlorophenoxyisobutyrate and betabenzalbutyrate

Robert G. Lamb , Patsy M. Hill , and Harold J. Fallon

Departments of Medicine and Pharmacology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27514

Palmitoyl CoA deacylase activity was measured in preparations of rat liver microsomes. Two hypolipidemic agents, chlorophenoxyisobutyrate and betabenzalbutyrate caused inhibition of palmitoyl CoA deacylase in vitro. The I50 values for chlorophenoxyisobutyrate and betabenzalbutyrate were 5.0 and 7.5 mm, respectively. The inhibition by both agents was reversible, and both drugs lowered the palmitoyl CoA-binding capacity of microsomes.

The deacylase reaction rate was maximum when the binding of palmitoyl CoA to soluble or microsomal protein was low. Addition of albumin to the reaction mixture resulted in greater binding of palmitoyl CoA to protein and a lower reaction rate. Inhibition of the deacylase by chlorophenoxyisobutyrate and betabenzalbutyrate also was greater when palmitoyl CoA was not protein bound. The inhibition of palmitoyl CoA deacylase by these hypolipidemic agents may contribute to their effects on lipid metabolism.

Supplementary key words binding • albumin • microsomes

Submitted on May 23, 1972
Revised on January 9, 1973
Accepted on March 8, 1973


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