Differential solubilization of proteins, phospholipids, and cholesterol of erythrocyte membranes by detergents
Autor: | F. H. Kirkpatrick, Stanley E. Gordesky, G.V. Marinetti |
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Rok vydání: | 1974 |
Předmět: |
Erythrocytes
Chromatography Paper Macromolecular Substances Biophysics Phospholipid Fractionation Biochemistry Micelle Surface-Active Agents chemistry.chemical_compound Methods Humans Colloids Phospholipids Chromatography Red Cell Cholesterol Phosphatidylethanolamines Cell Membrane Extraction (chemistry) Lysophosphatidylcholines Sodium Dodecyl Sulfate Blood Proteins Cell Biology Sphingomyelins Membrane Solubility chemistry Evaluation Studies as Topic Spectrophotometry Phosphatidylcholines Electrophoresis Polyacrylamide Gel lipids (amino acids peptides and proteins) Sphingomyelin Deoxycholic Acid |
Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 345:154-161 |
ISSN: | 0005-2736 |
DOI: | 10.1016/0005-2736(74)90254-5 |
Popis: | Red cell membranes were treated with increasing concentrations of Triton X-100, sodium dodecylsulfate, or sodium deoxycholate at pH 7.5, and the solubilization of total protein, total phospholipid, cholesterol, and of individual proteins and phospholipids was determined as a function of detergent concentration. The results suggest that each detergent solubilized membrane components by a different mechanism. Sodium dodecylsulfate extracted individual protein and lipids separately, each membrane component having a sigmoid extraction curve with a different dodecylsulfate concentration at midpoint. Sodium deoxycholate solubilized all proteins and phospholipids in parallel, with little fractionation, but cholesterol was not solubilized significantly until 60% of the protein and phospholipids were extracted. The data suggest that deoxycholate intially solubilizes membrane lipoproteins by displacement of cholesterol into the residual membrane matrix, followed at higher deoxycholate concentration by removal of phospholipids from both soluble and insoluble proteins into deoxycholate-phospholipid micelles which in turn solulibilize cholesterol. Triton X-100 initially solubilizes most proteins and lipids in parallel, but proteins are released faster while sphingomyelin is preferentially retained in the pellet. At higher Triton X-100 concentration, net protein solubilization ceases while residual lipids are completely solubilized. |
Databáze: | OpenAIRE |
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