CLIC-1 functions as a chloride channel when expressed and purified from bacteria.

@article{Tulk2000CLIC1FA,
  title={CLIC-1 functions as a chloride channel when expressed and purified from bacteria.},
  author={Barry M Tulk and Paul H Schlesinger and Suneil Kapadia and John C. Edwards},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 35},
  pages={26986-93}
}
CLIC-1 is a member of a family of proteins related to the bovine intracellular chloride channel p64 which has been proposed to function as a chloride channel. We expressed CLIC-1 as a glutathione S-transferase fusion protein in bacteria. The fusion protein was purified by glutathione affinity, and CLIC-1 was released from its fusion partner by digestion with thrombin. After further purification, CLIC-1 was reconstituted into phospholipid vesicles by detergent dialysis. Chloride permeability of… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 34 extracted citations

References

Publications referenced by this paper.
Showing 1-4 of 4 references

Functions as a Cl2 Channel 26993 by gest on Jne 26

E. M. Schwiebert, D. J. Benos, M. E. Egan, M. J. Stutts, W. B. Guggino
Physiol. Rev. 79, • 1999
View 1 Excerpt

Ion Channels of Excitable Membranes, pp. 183–216

B. Hille
Sinauer Associates, • 1992
View 1 Excerpt

Ion Channel Reconstitution (Miller, C, ed) pp. 533–552

M. Colombini
1986
View 2 Excerpts

Statistical Methods in Medical Research, pp. 189–207

P. Armitage
1971
View 1 Excerpt

Similar Papers

Loading similar papers…