| Autor: |
Kleyman, T. R., Kraehenbuhl, J. P., Rossier, B. C., Cragoe, E. J., Warnock, D. G. |
| Zdroj: |
American Journal of Physiology - Cell Physiology; December 1989, Vol. 257 Issue: 6 pC1135-C1141, 7p |
| Abstrakt: |
Most Na(+)-selective transport proteins are inhibited by the drug amiloride. Studies using amiloride analogues suggest that specific regions of amiloride might participate in binding to receptors on these transport proteins. To determine whether certain domains of this drug are recognized as distinct epitopes, amiloride was coupled to albumin through either its C-5 NH2-group on the pyrazine ring or through a terminal NH2-group of the guanidino moiety, and antibodies were raised against these amiloride-albumin conjugates. Studies of antibody binding to amiloride analogues identified the 3,5-diaminopyrazinyl, the guanidinocarbonyl, and the C-6 halo moieties as distinct epitopes, although the antibodies required the presence of both the 3,5-diaminopyrazinyl as well as the guanidinocarbonyl moiety for binding. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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