Subcellular location and topography of rat hepatic monoacylglycerol acyltransferase activity
| Autor: | Rosalind A. Coleman, E. B. Haynes |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Cell Membrane Permeability
Biophysics Pronase Biochemistry Substrate Specificity Endocrinology Endopeptidases Animals Differential centrifugation chemistry.chemical_classification Chymotrypsin biology Endoplasmic reticulum Cell Membrane Proteinase K Animals Suckling Rats Cytosol Enzyme chemistry Microsomes Liver biology.protein Microsome Acyltransferases Adenylyl Cyclases |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 834:180-187 |
| ISSN: | 0005-2760 |
| DOI: | 10.1016/0005-2760(85)90154-7 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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