|
||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
The Journal of General Physiology, Vol 74, 351-374, Copyright © 1979 by The Rockefeller University Press
ARTICLES |
RB Gunn and O Frohlich
The kinetics of chloride and bromide transport were examined in intact human red blood cells and resealed ghosts. Because the influx and efflux of halide ions are almost equal (less than 0.01% difference), the stimulation of the exchange flux by external halides could be determined by measuring 36Cl or 82Br efflux. When the external halide concentration was increased by replacement of isoionic, isotonic solutions of sucrose and the nontransported anion citrate, the stimulation of the exchange flux was hyperbolic and was maximum at 20 mM halide externally. The K 1/2-out, the external concentration of chloride or bromide which stimulated the efflux to half of its maximum value, was 3 and 1 mM respectively, 15-fold smaller than K 1/2-in which we found to be about equal to the K 1/2 of halide self-exchange with nearly equal internal and external concentrations. Thus, the transport mechanism behaves asymmetrically with respect to these transported halides. Bromide flux was two-fold greater in bromide-chloride heteroexchange than in bromide-bromide self-exchange but it was still much smaller than the chloride self-exchange flux. The maximum influx and efflux of bromide in exchange for chloride were roughly eqal. Thus, since the maximum transport rates in the two directions are nearly equal, the kinetics of bromide equilibrium exchange with equal concentrations on the two sides are controlled on the inside where K 1/2 is greatest. The K 1/2-out Cl was a hyperbolic function of internal chloride concentration and was proportional to the maximum flux at each internal chloride concentration. These results are evaluated in terms of two broad categories of models. We conclude that, in contrast to other ion transport systems which have been shown to have kinetics of a sequential mechanism, anion exchange is compatible with a ping-pong mechanism in which a single site reciprocates between inside- and outside-facing orientations with asymmetric K 1/2 values.
This article has been cited by other articles:
![]() |
M. N. Chernova, A. K. Stewart, P. N. Barry, M. L. Jennings, and S. L. Alper Mouse Ae1 E699Q mediates SO42-i/aniono exchange with [SO42-]i-dependent reversal of wild-type pHo sensitivity Am J Physiol Cell Physiol, August 1, 2008; 295(2): C302 - C312. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Pushkin and I. Kurtz SLC4 base (HCO3-, CO32-) transporters: classification, function, structure, genetic diseases, and knockout models Am J Physiol Renal Physiol, March 1, 2006; 290(3): F580 - F599. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. L. Jennings Evidence for a Second Binding/Transport Site for Chloride in Erythrocyte Anion Transporter AE1 Modified at Glutamate 681 Biophys. J., April 1, 2005; 88(4): 2681 - 2691. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. A. Knauf, F.-Y. Law, T.-W. V. Leung, A. U. Gehret, and M. L. Perez Substrate-dependent reversal of anion transport site orientation in the human red blood cell anion-exchange protein, AE1 PNAS, August 6, 2002; 99(16): 10861 - 10864. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Chang and T. Fujita A numerical model of acid-base transport in rat distal tubule Am J Physiol Renal Physiol, August 1, 2001; 281(2): F222 - F243. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. M. Weinstein A mathematical model of the outer medullary collecting duct of the rat Am J Physiol Renal Physiol, July 1, 2000; 279(1): F24 - F45. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Bahar, C. T. Gunter, C. Wu, S. D. Kennedy, and P. A. Knauf Persistence of external chloride and DIDS binding after chemical modification of Glu-681 in human band 3 Am J Physiol Cell Physiol, October 1, 1999; 277(4): C791 - C799. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. T. Timmer and R. B. Gunn Inducible expression of erythrocyte band 3 protein Am J Physiol Cell Physiol, January 1, 1999; 276(1): C66 - C75. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Fu, R. I. Sarker, K. Abe, E. Bolton, and P. C. Maloney Structure/Function Relationships in OxlT, the Oxalate-Formate Transporter of Oxalobacter formigenes. ASSIGNMENT OF TRANSMEMBRANE HELIX 11 TO THE TRANSLOCATION PATHWAY J. Biol. Chem., March 16, 2001; 276(12): 8753 - 8760. [Abstract] [Full Text] [PDF] |
||||
|
|