Incorporation of hormone-sensitive lipase into phosphatidylcholine vesicles
| Autor: | Gudrun Fredrikson, Roger Sundler, Cecilia Holm, Per Belfrage |
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| Rok vydání: | 1990 |
| Předmět: |
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Detergents Triacylglycerol lipase Phospholipid Biochemistry Gel permeation chromatography chemistry.chemical_compound Chaps Phosphatidylcholine Animals Scattering Radiation Lipase Liposome Chromatography biology Vesicle Organic Chemistry food and beverages Cholic Acids Dextrans Membranes Artificial Cell Biology Sterol Esterase Rats Microscopy Electron chemistry Phosphatidylcholines biology.protein Electrophoresis Polyacrylamide Gel Carboxylic Ester Hydrolases Dialysis |
| Zdroj: | Lipids. 25:254-259 |
| ISSN: | 1558-9307 0024-4201 |
| DOI: | 10.1007/bf02544384 |
| Popis: | Enzymatically active, detergent-solubilized purified hormone-sensitive lipase (HSL) was incorporated into phosphatidylcholine (PC) vesicles, using a detergent-dialysis procedure with small PC vesicles, obtained by sonication, as phospholipid source and CHAPS, a zwitterionic bile-salt derivative, as detergent. Association of enzyme protein with the PC vesicles was verified by floatation in a discontinuous dextran gradient and by gel chromatography. An average of 35% of added HSL was incorporated into the vesicles. The vesicles were shown, by quasi-elastic light scattering and electron microscopy, to have a diameter of approximately 160 nm. The vesicle-associated HSL could be phosphorylated by cyclic AMP-dependent protein kinase. The vesicles were stable, both with regard to enzyme activity and size, for at least 4 days when stored at 4 degrees C. The preparation of detergent-free, vesicle-associated and stable HSL provides new possibilities to study some of its properties, and supports and extends the previous report (Holm, C., Fredrikson, G., and Belfrage, P., J. Biol. Chem. 261, 15659-15661, 1986) which demonstrated the amphiphilic character of HSL. |
| Databáze: | OpenAIRE |
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