Functional size of acyl coenzyme A:diacylglycerol acyltransferase by radiation inactivation
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Updated: Aug 2, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
S Ozasa1, E S Kempner, S K Erickson
1Division of Gastroenterology, Stanford University School of Medicine, CA 94305.
Abstract:
Rat liver acyl coenzyme A:diacylglycerol acyltransferase, an intrinsic membrane activity associated with the endoplasmic reticulum, catalyzes the terminal and rate-limiting step in triglyceride synthesis. This enzyme has never been purified nor has its gene been isolated. Inactivation by ionizing radiation and target analysis were used to determine its functional size in situ. Monoexponential radiation inactivation curves were obtained which indicated that a single-sized unit of 72 +/- 4 kDa is required for expression of activity. The size corresponds only to the protein portion of the target and may represent one or several polypeptides.
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