The preparation of hydrophilic derivatives of band 3 protein by acylation of 
the human red blood cell membrane

Herbst, Franz; Rudloff, Victor

doi:10.1515/bchm2.1984.365.1.525

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The preparation of hydrophilic derivatives of band 3 protein by acylation of the human red blood cell membrane

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Herbst, Franz
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Rudloff, Victor
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Herbst, F., & Rudloff, V. (1984). The preparation of hydrophilic derivatives of band 3 protein by acylation of the human red blood cell membrane. Hoppe-Seyler's Zeitschrift für physiologische Chemie, 365(5), 525-530. doi:10.1515/bchm2.1984.365.1.525.

Cite as: https://hdl.handle.net/21.11116/0000-0008-6E1B-0

Abstract

In situ reaction of erythrocyte membranes with dicarboxylic anhydrides leads to solubilization of hydrophobic integral proteins. Removal of peripheral proteins and bulk lipid by appropriate sedimentation and dialysis steps yields hydrophilic band 3 protein derivatives. These acyl compounds display size heterogeneity upon gel filtration. A chromatographically homogeneous acyl band 3 protein is obtained if the acylation is conducted in the presence of detergent and the detergent subsequently removed. Hydrophilic acyl derivatives of band 3 protein can be subjected to conventional analytical techniques without the use of detergents.