Abstract
A Cl- channel protein of sarcoplasmic reticulum (SR) was purified by assaying the channel activity in a planar lipid bilayer system. The light fraction of SR vesicles was solubilized in CHAPS and fractionated by anion exchange, gel filtration, and affinity chromatography with concanavalin A. All fractions in each step were reconstituted into vesicles with asolectin by dialysis and their channel activities were assayed after the vesicles had been fused into a planar lipid bilayer. A 100-kDa protein, different from Ca2+-ATPase, was found to form anion channels.
| Original language | English |
|---|---|
| Pages (from-to) | 38-44 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 176 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Apr 15 1991 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Ide, T., Sakamoto, H., Morita, T., Taguchi, T., & Kasai, M. (1991). Purification of A Cl--channel protein of sarcoplasmic reticulum by assaying the channel activity in the planar lipid bilayer system. Biochemical and Biophysical Research Communications, 176(1), 38-44. https://doi.org/10.1016/0006-291X(91)90886-C