## Abstract Treatment of isolated human erythrocyte membranes with Triton Xβ100 at ionic strength β0.04 preferentially released all the glycerolipid and glycoprotein species. At low ionic strength, certain nonglycosylated polypeptides were also selectively solubilized. The liberated polypeptides we
Interactions between proteins and lipids from human red cell membranes
β Scribed by R.F.A. Zwaal; L.L.M. van Deenen
- Publisher
- Elsevier Science
- Year
- 1970
- Tongue
- English
- Weight
- 542 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0009-3084
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β¦ Synopsis
A method is described for the recombination of total lipids or phospholipids with apoproteins from human red cell membranes. 1. Recombinations turned out to be possible with negatively charged sonicated lipids and positively charged proteins, in between pH 3.5 and 4.5. For this purpose the sialic acid was removed from either the proteins or the intact erythrocytes by treatment with neuraminidase. 2. The stoichiometry of the reaction appeared to be dependent on pH. The differences in lipid uptake by apoproteins was compared, in dependency from the pH, with the differences in uptake of additional lipids by sonicated ghost suspensions and lipoprotein solutions derived from human erythrocytes. 3. Recombinations with individual phospholipids confirm that opposite charges of lipids and proteins are essential for the initial interaction. 4. It is considered to be likely that in addition hydrophobic associations between proteins and lipids are formed.
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