The functional size of acyl-coenzyme A (CoA):cholesterol acyltransferase and acyl-CoA hydrolase as determined by radiation inactivation

Journal Article · Fri May 25 04:00:00 EDT 1990 · Journal of Biological Chemistry; (USA)

OSTI ID:7043402

Billheimer, J T; Cromley, D A; Kempner, E S ^[1]

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1. E. I. du Pont de Nemours Co., Inc., Wilmington, DE (USA)

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.

• OSTI ID: 7043402
• Journal Information: Journal of Biological Chemistry; (USA), Journal Name: Journal of Biological Chemistry; (USA) Vol. 265:15; ISSN JBCHA; ISSN 0021-9258
• Country of Publication: United States
• Language: English

Related Subjects

560120* -- Radiation Effects on Biochemicals
Cells
& Tissue Culture
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ANIMALS
BODY
CELL CONSTITUENTS
CHEMICAL RADIATION EFFECTS
CHEMICAL REACTIONS
CHEMISTRY
CHOLESTEROL
DIGESTIVE SYSTEM
DOSE-RESPONSE RELATIONSHIPS
ELECTRONS
ELEMENTARY PARTICLES
ENDOPLASMIC RETICULUM
ENZYME ACTIVITY
ENZYMES
ESTERIFICATION
FERMIONS
GLANDS
HYDROLASES
HYDROXY COMPOUNDS
INHIBITION
LEPTONS
LIVER
MAMMALS
MICROSOMES
MOLECULAR WEIGHT
ORGANIC COMPOUNDS
ORGANOIDS
ORGANS
RADIATION CHEMISTRY
RADIATION EFFECTS
RATS
RIBOSOMES
RODENTS
STEROIDS
STEROLS
TRANSFERASES
VERTEBRATES