Removal of nonionic detergent from proteins fractionated by electrofocusing
✍ Scribed by Peter Strålfors; Hans Tornqvist; Bengt Jergil; Per Belfrage
- Book ID
- 113125885
- Publisher
- Elsevier Science
- Year
- 1978
- Weight
- 470 KB
- Volume
- 533
- Category
- Article
- ISSN
- 0005-2795
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📜 SIMILAR VOLUMES
## Abstract Treatment of isolated human erythrocyte membranes with Triton X‐100 at ionic strength ⋍0.04 preferentially released all the glycerolipid and glycoprotein species. At low ionic strength, certain nonglycosylated polypeptides were also selectively solubilized. The liberated polypeptides we
The plasma membrane of erythrocytes, as of other cells, is thought to act as the barrier responsible for maintaining intracellular gradients of most ions and small molecular species between the cell and its environment. Controlled application of the nonionic detergent Brij 58 effectively opened the
Hydrophobic zeolite Y was used to adsorb detergents from protein solutions and within one minute the commonly used detergents sodium dodecyl sulfate, cetyl trimethyl ammonium bromide, and Triton X-100 at concentrations of 10 mg/ml were adsorbed to a level below their critical micelle concentrations.