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人红细胞血影中氯离子转运系统的不对称性。

Asymmetry of the chloride transport system in human erythrocyte ghosts.

作者信息

Schnell K F, Besl E, Manz A

出版信息

Pflugers Arch. 1978 Jun 21;375(1):87-95. doi: 10.1007/BF00584152.

DOI:10.1007/BF00584152
PMID:567343
Abstract

The concentration dependence of the unidirectional chloride flux and the inhibition of the unidirectional chloride flux by sulfate were studied in human red cell ghosts. The concentration dependence of the unidirectional chloride flux and its inhibition by sulfate were asymmetric. The unidirectional chloride flux can be saturated from the inner and from the outer membrane surface. For the inner membrane surface, lower chloride half-saturation constants were obtained than for the outer membrane surface. The inhibition of the unidirectional chloride flux by sulfate is competitive. In contrast to the chloride half-saturation constants, the inhibition constants of sulfate for the inner membrane surface were higher than the inhibition constants of sulfate for the outher membrane surface. Either there are fixed anion binding sites at the inner and at the outer membrane surface which control the access of anions to a pore, or there is a mobile carrier which is in contact with both membrane surfaces. The asymmetry of the concentration response and of the inhibition of the unidirectional chloride flux suggest that the anion binding sites at the inner and at the outer membrane surface differ with respect to their affinities for chloride and for sulfate. Alternatively, the asymmetry of the chloride transport system could indicate an asymmetric distribution of a mobile anion carrier across the erythrocyte membrane.

摘要

在人红细胞血影中研究了单向氯离子通量的浓度依赖性以及硫酸盐对单向氯离子通量的抑制作用。单向氯离子通量的浓度依赖性及其受硫酸盐的抑制作用是不对称的。单向氯离子通量可从内膜表面和外膜表面达到饱和。对于内膜表面,获得的氯离子半饱和常数低于外膜表面。硫酸盐对单向氯离子通量的抑制是竞争性的。与氯离子半饱和常数相反,硫酸盐对内膜表面的抑制常数高于对内膜表面的抑制常数。要么在内膜表面和外膜表面存在固定的阴离子结合位点,控制阴离子进入孔道,要么存在与两个膜表面都接触的移动载体。浓度响应和单向氯离子通量抑制的不对称性表明,内膜表面和外膜表面的阴离子结合位点对氯离子和硫酸盐的亲和力不同。或者,氯离子转运系统的不对称性可能表明移动阴离子载体在红细胞膜上的不对称分布。

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1
Asymmetry of the chloride transport system in human erythrocyte ghosts.人红细胞血影中氯离子转运系统的不对称性。
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引用本文的文献

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J Gen Physiol. 1983 Mar;81(3):421-49. doi: 10.1085/jgp.81.3.421.
2
Relationship of net chloride flow across the human erythrocyte membrane to the anion exchange mechanism.跨人红细胞膜的净氯流与阴离子交换机制的关系。
J Gen Physiol. 1983 Jan;81(1):95-126. doi: 10.1085/jgp.81.1.95.
3
Use of niflumic acid to determine the nature of the asymmetry of the human erythrocyte anion exchange system.使用氟尼辛来确定人类红细胞阴离子交换系统不对称性的性质。

本文引用的文献

1
Temperature dependence of chloride, bromide, iodide, thiocyanate and salicylate transport in human red cells.人体红细胞中氯离子、溴离子、碘离子、硫氰酸盐和水杨酸盐转运的温度依赖性
J Physiol. 1972 Aug;224(3):583-610. doi: 10.1113/jphysiol.1972.sp009914.
2
The effect of pH at hemolysis on the reconstitution of low cation permeability in human erythrocyte ghosts.溶血时的pH值对人红细胞膜空壳低阳离子通透性重建的影响。
Biochim Biophys Acta. 1972 Feb 11;255(2):696-702. doi: 10.1016/0005-2736(72)90174-5.
3
Membrane proteins related to anion permeability of human red blood cells. II. Effects of proteolytic enzymes on disulfonic stilbene sites of surface proteins.
J Gen Physiol. 1984 May;83(5):703-25. doi: 10.1085/jgp.83.5.703.
4
Effects of the transport site conformation on the binding of external NAP-taurine to the human erythrocyte anion exchange system. Evidence for intrinsic asymmetry.转运位点构象对外部NAP-牛磺酸与人红细胞阴离子交换系统结合的影响。内在不对称性的证据。
J Gen Physiol. 1984 May;83(5):683-701. doi: 10.1085/jgp.83.5.683.
5
Transmembrane effects of intracellular chloride on the inhibitory potency of extracellular H2DIDS. Evidence for two conformations of the transport site of the human erythrocyte anion exchange protein.细胞内氯离子对细胞外H2DIDS抑制效力的跨膜效应。人红细胞阴离子交换蛋白转运位点两种构象的证据。
J Gen Physiol. 1984 May;83(5):657-81. doi: 10.1085/jgp.83.5.657.
6
Concentration dependence of the unidirectional sulfate and phosphate flux in human red cell ghosts under selfexchange and under homoexchange conditions.在自交换和同型交换条件下,人红细胞膜空壳中单向硫酸根和磷酸根通量的浓度依赖性。
Pflugers Arch. 1984 Oct;402(2):197-206. doi: 10.1007/BF00583335.
7
Concentration dependence of the chloride selfexchange and homoexchange fluxes in human red cell ghosts.人体红细胞血影中氯离子自交换和同离子交换通量的浓度依赖性
Pflugers Arch. 1985 Oct;405(3):193-201. doi: 10.1007/BF00582560.
8
DMO-transport in human red blood cells.二甲基亚砜在人类红细胞中的转运
Pflugers Arch. 1986 Jun;406(6):568-73. doi: 10.1007/BF00584022.
9
Characterization of the Band 3 substrate site in human red cell ghosts by NDS-TEMPO, a disulfonatostilbene spin probe: the function of protons in NDS-TEMPO and substrate-anion binding in relation to anion transport.用二磺化芪自旋探针NDS-TEMPO对人红细胞血影中带3底物位点的表征:NDS-TEMPO中质子的功能以及与阴离子转运相关的底物-阴离子结合
J Membr Biol. 1986;91(2):129-46. doi: 10.1007/BF01925790.
10
Inhibition of the phosphate self-exchange flux in human erythrocytes and erythrocyte ghosts.对人红细胞及红细胞影中磷酸自交换通量的抑制作用。
J Membr Biol. 1990 Oct;118(1):19-47. doi: 10.1007/BF01872202.
与人类红细胞阴离子通透性相关的膜蛋白。II. 蛋白水解酶对表面蛋白二磺酸芪位点的影响。
J Membr Biol. 1974;15(3):227-48. doi: 10.1007/BF01870089.
4
Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation.与人类红细胞阴离子通透性相关的膜蛋白。I. 二磺酸芪结合位点在参与通透的蛋白质中的定位。
J Membr Biol. 1974;15(3):207-26. doi: 10.1007/BF01870088.
5
Characteristics of chloride transport in human red blood cells.人类红细胞中氯离子转运的特征
J Gen Physiol. 1973 Feb;61(2):185-206. doi: 10.1085/jgp.61.2.185.
6
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J Membr Biol. 1972;8(1):1-26. doi: 10.1007/BF01868092.
7
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Nat New Biol. 1973 Jul 11;244(132):47-9. doi: 10.1038/newbio244047a0.
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Effects of halides and bicarbonate on chloride transport in human red blood cells.卤化物和碳酸氢盐对人红细胞中氯离子转运的影响。
J Gen Physiol. 1976 Feb;67(2):223-34. doi: 10.1085/jgp.67.2.223.
9
Sidedness of the inhibitory action of disulfonic acids on chloride equilibrium exchange and net transport across the human erythrocyte membrane.二磺酸对氯离子平衡交换及跨人红细胞膜净转运的抑制作用的方向性
FEBS Lett. 1976 Feb 15;62(2):182-5. doi: 10.1016/0014-5793(76)80048-8.
10
Chemical modification of membrane proteins in relation to inhibition of anion exchange in human red blood cells.与人类红细胞中阴离子交换抑制相关的膜蛋白化学修饰
J Cell Physiol. 1975 Dec;86(3 Pt 1):471-94. doi: 10.1002/jcp.1040860305.