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Purification and Reconstitution of Chloride Channels from Kidney and Trachea
Abstract
Chloride channels mediate absorption and secretion of fluid in epithelia, and the regulation of these channels is now known to be defective in cystic fibrosis. Indanyl-oxyacetic acid 94 (IAA-94) is a high-affinity ligand for the chloride channel, and an affinity resin based on that structure was developed. Solubilized proteins from kidney and trachea membranes were applied to the affinity matrix, and four proteins with apparent molecular masses of 97, 64, 40, and 27 kilodaltons were eluted from the column by excess IAA-94. A potential-dependent 36Cl- uptake was observed after reconstituting these proteins into liposomes. Three types of chloride channels with single-channel conductances of 26, 100, and 400 picosiemens were observed after fusion of these liposomes with planar lipid bilayers. Similar types of chloride channels have been observed in epithelia.
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Cited by
Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNA
Riordan, J. R., Rommens, J. M., Kerem, B.-S., Alon, N., Rozmahel, R., Grzelczak, Z., Zielenski, J., Lok, S., Plavsic, N., Chou, J.-L., et al. (1989) · Science · doi:10.1126/science.2475911 · Cited by 7,418
Molecular Structure and Physiological Function of Chloride Channels
Jentsch, T. J., Stein, V., Weinreich, F., & Zdebik, A. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00029.2001 · Cited by 1,256
Metadata
- Authors
- Landry, D. W., Akabas, M. H., Redhead, C., Edelman, A., Cragoe, E. J., & Al-Awqati, Q.
- Venue
- Science
- Published
- 1989-06-23
- Volume
- 244
- Issue
- 4911
- Pages
- 1469-1472
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2084647191
- Cited by
- 182
- References
- 0
- FWCI
- 7.94
- Type
- journal article
- Language
- en
- Open access
- closed
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- Landry, D. W., Akabas, M. H., Redhead, C., Edelman, A., Cragoe, E. J., & Al-Awqati, Q. (1989). Purification and Reconstitution of Chloride Channels from Kidney and Trachea. Science. https://doi.org/10.1126/science.2472007
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