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Journal Article

Interactions of band 3-protein from human erythrocyte membranes with cholesterol and cholesterol analogues

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Klappauf,  Eberhard
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Klappauf, E., & Schubert, D. (1979). Interactions of band 3-protein from human erythrocyte membranes with cholesterol and cholesterol analogues. Hoppe-Seyler's Zeitschrift für physiologische Chemie, 360(9), 1225-1235. doi:10.1515/BCHM2.1979.360.2.1225.


Cite as: https://hdl.handle.net/21.11116/0000-0008-608E-C
Abstract
The interaction between cholesterol and band 3-protein from human erythrocyte membranes was studied by incorporating the solubilized protein into monolayers of cholesterol and related sterols at the air-water interface and measuring the changes in surface pressure which accompanied protein incorporation. The following results were obtained: 1) Band 3-protein shows a very strong interaction with cholesterol monolayers. Both apolar and polar bonds contribute to this interaction. 2) Steroids with a structure slightly different from that of cholesterol (especially with respect to the polar group and the side chain) in most cases show a reduced affinity for band 3-protein. Thus, the protein-sterol interaction is highly specific. It is assumed that the protein-cholesterol interaction can be subidivided into two parts: an unspecific one which results from contributions from several sterol molecules, and a specific one which is due to the high affinity binding of the protein and cholesterol. The structural element responsible for the high affinity interaction is assumed to be a sterol-binding niche on the surface of band 3-protein. The sterol is thought to be held in the niche by a hydrogen bond at its polar head and a variety of hydrophobic bonds along its ring system and side chain.