Published May 25, 1990
| Version v1
Journal article
The functional size of acyl-coenzyme A (CoA):cholesterol acyltransferase and acyl-CoA hydrolase as determined by radiation inactivation
- 1. E. I. du Pont de Nemours ampersand Co., Inc., Wilmington, DE (USA)
Description
Frozen rat liver microsomes and rough endoplasmic reticulum were irradiated with high energy electrons. The surviving enzymatic activity of acyl-CoA:cholesterol acyltransferase and activity for esterification of 25-hydroxycholesterol decreased as a simple exponential function of radiation exposure, leading to a target size of 170-180 kDa. The loss of acyl-CoA hydrolase activity with a radiation dose was complex and resolved as a 45-kDa enzyme associated with a large inhibitor. It is interpreted that acyl-CoA hydrolase is the acyl-CoA-binding component and the inhibitor is the cholesterol-binding component of acyl-CoA:cholesterol acyltransferase
Additional details
Publishing Information
- Journal Title
- Journal of Biological Chemistry
- Journal Volume
- 265
- Journal Issue
- 15
- Series
- J. Biol. Chem.
- Journal Page Range
- 8632-8635
- ISSN
- 0021-9258
- CODEN
- JBCHA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 21074768
- Subject category
- S63: RADIATION, THERMAL, AND OTHER ENVIRONMENTAL POLLUTANT EFFECTS ON LIVING ORGANISMS AND BIOLOGICAL MATERIALS;
- Descriptors DEI
- CHEMICAL RADIATION EFFECTS; CHOLESTEROL; DOSE-RESPONSE RELATIONSHIPS; ELECTRONS; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ESTERIFICATION; HYDROLASES; INHIBITION; LIVER; MICROSOMES; MOLECULAR WEIGHT; RATS; TRANSFERASES
- Descriptors DEC
- ANIMALS; BODY; CELL CONSTITUENTS; CHEMICAL REACTIONS; DIGESTIVE SYSTEM; ELEMENTARY PARTICLES; ENZYMES; FERMIONS; GLANDS; HYDROXY COMPOUNDS; LEPTONS; MAMMALS; ORGANIC COMPOUNDS; ORGANOIDS; ORGANS; RADIATION EFFECTS; RODENTS; STEROIDS; STEROLS; VERTEBRATES