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  • Title: Subcellular location and topography of rat hepatic monoacylglycerol acyltransferase activity.
    Author: Coleman RA, Haynes EB.
    Journal: Biochim Biophys Acta; 1985 Apr 25; 834(2):180-7. PubMed ID: 3888275.
    Abstract:
    Monoacylglycerol acyltransferase activity from suckling rat liver was localized to the microsomal subcellular fraction by differential centrifugation and comparison with the partitioning of selected marker enzymes. Chymotrypsin, pronase, and proteinase K inactivated the monoacylglycerol acyltransferase activity in detergent-disrupted microsomes, but not in intact microsomes, falsely suggesting a lumenal location for the enzyme. The impermeant inhibitors mercury-dextran and 4,4'-diisothiocyano,-2,2'-disulfonic acid stilbene inhibited monoacylglycerol acyltransferase in intact microsomes. These data, as well as the lack of latency and the inability of the substrate palmitoyl-CoA to readily permeate hepatic microsomes from suckling rats, strongly suggest that the enzyme's active site faces the cytosolic surface of the endoplasmic reticulum.
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