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

Journal Article · Fri May 25 00:00:00 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), Vol. 265:15; ISSN 0021-9258
• Country of Publication: United States
• Language: English

Related Subjects

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