IONIC PERMEABILITY OF ADSORBED MEMBRANE-PROTEIN MONOLAYERS

被引:6
作者
BLANK, M
SOO, L
ABBOTT, RE
机构
[1] Department of Physiology, Columbia University
关键词
anion; membrane; pH;
D O I
10.1149/1.2129309
中图分类号
O646 [电化学、电解、磁化学];
学科分类号
081704 ;
摘要
Spectrin and actin (S+A) are important extrinsic membrane proteins that are present as a layer on the inner face of the erythrocyte membrane. Using the polarographic technique, we have studied the ion permeability of adsorbed S+A monolayers at the mercury/water interface. The relative permeability of the S+A layer to cations and anions at different pH's is consistent with an isoelectric point (IEP) at a pH between 5 and 6. Below the IEP, the layer tends to impede the flow of cations. Above the IEP, the S+A layer impedes anions. Extrapolating to pH 7.4, it appears that the S+A layer is relatively impermeable to anions in the range where the erythrocyte membrane as a whole is very permeable to anions. The permeabilities of complete S+A monolayers to the CU++ complexes are estimated to be on the order of 10-4 cm/sec. Our observations indicate the existence of an anion-depleted compartment at the inner surface of the membrane, and suggest that the specialized anion carriers in the membrane penetrate this layer. © 1979, The Electrochemical Society, Inc. All rights reserved.
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页码:1471 / 1474
页数:4
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