Transient low-affinity agonist binding to Torpedo postsynaptic membranes resolved by using sequential mixing stopped-flow fluorescence spectroscopy

Biochemistry

Volumn 37, Issue 3, 1998, Pages 956-964

  Raines, Douglas E ^a   Krishnan, Nanditha S ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINIC AGENT; NICOTINIC RECEPTOR;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; ISOMERISM; NONHUMAN; POSTSYNAPTIC MEMBRANE; PRIORITY JOURNAL; PROTEIN CONFORMATION; RECEPTOR AFFINITY; RECEPTOR BINDING; TORPEDO;

ANIMALS; BINDING SITES; DANSYL COMPOUNDS; FLUORESCENT DYES; ION CHANNELS; MODELS, CHEMICAL; OCTANOLS; PROTEIN CONFORMATION; QUATERNARY AMMONIUM COMPOUNDS; RECEPTORS, CHOLINERGIC; SPECTROMETRY, FLUORESCENCE; SYNAPTIC MEMBRANES; TORPEDO;

ANIMALIA;

EID: 0032548470     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971689w     Document Type: Article

References (32)

1. Lingle, C. J., Maconochie, D., and Steinbach, J. H. (1992) J. Membr. Biol. 126, 195-217.
2. Stroud, R. M., McCarthy, M. P., and Shuster, M. (1990) Biochemistry 29, 11009-11023.
3. Jackson, M. B. (1988) J. Physiol. 397, 555-583.
4. Sine, S. M., Claudio, T., and Sigworth, F. J. (1990) J. Gen. Physiol. 96, 395-437.
5. Forman, S. A., Firestone, L. L., and Miller, K. W. (1987) Biochemistry 26, 2807-2814.
6. Forman, S. A., and Miller, K. W. (1988) Biophys. J. 54, 149-158.
7. Takeyasu, K., Shiono, S., Udgaonkar, J. B., Fujita, N., and Hess, G. P. (1986) Biochemistry 25, 1770-1776.
8. Feltz, A., and Trautmann, A. (1982) J. Physiol. 322, 257-272.
9. Walker, J. W., Takeyasu, K., and McNamee, M. G. (1982) Biochemistry 21, 5384-5389.
10. Neubig, R. R., Boyd, N. D., and Cohen, J. B. (1982) Biochemistry 21, 3460-3467.
11. Boyd, N. D., and Cohen, J. B. (1980) Biochemistry 19, 5344-5353.
12. Heidmann, T., and Changeux, J. P. (1979) Eur. J. Biochem. 94, 255-279.
13. Heidmann, T., Bernhardt, J., Neumann, E., and Changeux, J. P. (1983) Biochemistry 22, 5452-5459.
14. Dilger, J. P., and Liu, Y. (1992) Pflugers Arch. 420, 479-485.
15. Prinz, H., and Maelicke, A. (1992) Biochemistry 31, 6728-6738.
16. Heidmann, T., and Changeux, J. P. (1980) Biochem. Biophys. Res. Commun. 97, 889-896.
17. Braswell, L. M., Miller, K. W., and Sauter, J. F. (1984) Br. J. Pharmacol. 83, 305-311.
18. Neubig, R. R., and Cohen, J. B. (1979) Biochemistry 18, 5464-5475.
19. Waksman, G., Fournie, Z. M. C., and Roques, B. (1976) FEBS Lett. 67, 335-342.
20. Firestone, L. L., Alifimoff, J. K., and Miller, K. W. (1994) Mol. Pharmacol. 46, 508-515.
21. Christensen, U., and Molgaard, L. (1991) FEBS Lett. 278, 204-206.
22. Liu, Y., and Dilger, J. P. (1991) Biophys. J. 60, 424-432.
23. Sine, S. M., and Steinbach, J. H. (1987) J. Physiol. 385, 325-359.
24. Jackson, M. B. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 2199-2203.
25. Johnson, D. A., Brown, R. D., Herz, J. M., Bermann, H. A., Andreasen, G. L., and Taylor, P. (1987) J. Biol. Chem. 262, 14022-14029.
26. Tonner, P. H., Wood, S. C., and Miller, K. W. (1992) Mol. Pharmacol. 42, 890-897.
27. Liu, Y., and Dilger, J. P. (1993) Synapse 13, 57-62.
28. Rankin, S. E. (1995) in Biological Sciences, p 166, Oxford University, Oxford, U.K.
29. Quast, U., Schimerlik, M. I., and Raftery, M. A. (1979) Biochemistry 18, 1891-1901.
30. Grunhagen, H. H., Iwatsubo, M., Changeux, J. P. (1977) Eur. J. Biochem. 80, 225-242.
31. Colquhoun, D., and Ogden, D. C. (1988) J. Physiol. 395, 131-159.
32. Wu, G., and Miller, K. W. (1994) Biochemistry 33, 9085-9091.