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Acylation of Integral Erythrocyte Membrane Proteins Resulting in a Soluble form of Band 3 Protein

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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. (1982). Acylation of Integral Erythrocyte Membrane Proteins Resulting in a Soluble form of Band 3 Protein. In Protides of the Biological Fluids (pp. 113-116). Oxford and New York: Pergamon Press. doi:10.1016/B978-0-08-027988-6.50027-6.


Cite as: http://hdl.handle.net/21.11116/0000-0007-DE25-6
Abstract
By repetetive acylation up to two-thirds of the integral proteins of the RBC membrane may be solubilized. The release of proteins from particulate material into supernatant phase is proportional to the release of protein-bound 3H2DIDS. Gel filtration of the solubilized acylated integral proteins in detergent-free media indicates a strong aggregation of band 3 protein. LiDS/Sepharose-chromatography gives a very similar elution profile for the integral protein components originating from soluble and particulate fraction. Amino acid analyses and fragmentation patterns of the two band 3 protein fractions show no significant differences.