Structural and Functional Properties of the Anion Transport System Isolated from Human Erythrocyte Membranes

Cabantchik, Z. I.; Wolosin, J. Mario; Ginsburg, H.; Zemel, O.

doi:10.1007/978-3-642-66564-6_24

Cited by 8 publications

(3 citation statements)

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“…The intracellular pH and R m were calculated from the chloride distribution and the extracellular pH as indicated in the methods section by using Eqs. (5) and (6). In amphotericin B treated red cells, pI-I(in) and pH(ex) are slightly different, but the differences are much smaller than in intact cells.…”

Section: \2mentioning

confidence: 93%

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Phosphate transport in human red blood cells: Concentration dependence and pH dependence of the unidirectional phosphate flux at equilibrium conditions

1981

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The concentration dependence and the pH dependence of the phosphate transport across the red cell membrane were investigated. The unidirectional phosphate fluxes were determined by measuring the 32P-phosphate self-exchange in amphotericin B (5 mumol/liter) treated erythrocytes at 25 degrees C. The flux/concentration curves display an S-shaped increase at low phosphate concentrations, a concentration optimum in the range of 150 to 200 mM phosphate and a self-inhibition at high phosphate concentrations. The apparent half-saturation concentrations, P(0.5), range from 50 to 70 mM and are little affected by pH. The self-inhibition constants, as far as they can be estimated, range from 400 to 600 mM. The observed maximal phosphate fluxes exhibit a strong pH dependence. At pH 7.2, the actual maximal flux is 2.1 X 10(-6) moles . min-1 . g cells-1. The ascending branches of the flux/concentration curves were fitted to the Hill equation. The apparent Hill coefficients were always in the range of 1.5-2.0. The descending branches of the flux/concentration curves appear to follow the same pattern of concentration response. The flux/pH curves were bell-shaped and symmetric with regard to their pH dependence. The pH optimum is at approximately pH 6.5-6.7. The apparent pK of the activator site is in the range of 7.0 to 7.2, while the apparent pK for the inactivating site is in the range of 6.2 to 6.5. The pK-values were not appreciably affected by the phosphate concentration. According to our studies, the transport system possesses two transport sites and probably two modifier sites as indicated by the apparent Hill coefficients. In addition, the transport system has two proton binding sites, one with a higher pK that activates and one with a lower pK that inactivates the transport system. Since our experiments were executed under self-exchange conditions, they do not provide any information concerning the location of these sites at the membrane surfaces.

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Section: \2mentioning

confidence: 93%

“…The intracellular phosphate concentrations P(i,l and the intracellular pH(i,~ were calculated according Eqs. (5) and (6). For details, see the methods section.…”

Section: Concentration Dependence Of the Unidirectional Phosphate Fluxmentioning

confidence: 99%

Phosphate transport in human red blood cells: Concentration dependence and pH dependence of the unidirectional phosphate flux at equilibrium conditions

1981

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“…Recently, the detergent Triton X-100 was used for the solubilization of human erythrocyte membranes and the resolution of their anion exchange system [4] as well as for the reconstitution of the glucose transport system [5]. Triton X-100 was used for solubilization of Semliki Fores?…”

Section: Introductionmentioning

confidence: 99%

An efficient method for reassembly of fusogenic sendai virus envelopes after solubilization of intact virions with triton X‐100

Volsky

Loyter

1978

FEBS Letters

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Transport systems of isolated hepatocytes

Schwenk

1980

Arch. Toxicol.

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Structural and Functional Properties of the Anion Transport System Isolated from Human Erythrocyte Membranes

Cited by 8 publications

References 20 publications

Phosphate transport in human red blood cells: Concentration dependence and pH dependence of the unidirectional phosphate flux at equilibrium conditions

Phosphate transport in human red blood cells: Concentration dependence and pH dependence of the unidirectional phosphate flux at equilibrium conditions

An efficient method for reassembly of fusogenic sendai virus envelopes after solubilization of intact virions with triton X‐100

Transport systems of isolated hepatocytes

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