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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-DE25-6 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-DE26-5
Genre: Book Chapter

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 Creators:
Herbst, Franz1, Author           
Rudloff, Victor1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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Free keywords: Erythrocyte membrane; protein acylation; band 3 protein; anion-transport protein
 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.

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Language(s): eng - English
 Dates: 2014-06-271982-05
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/B978-0-08-027988-6.50027-6
 Degree: -

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Title: Protides of the Biological Fluids
Source Genre: Series
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Publ. Info: Oxford and New York : Pergamon Press
Pages: 984 Volume / Issue: 29 Sequence Number: - Start / End Page: 113 - 116 Identifier: ISBN: 978-0-08-027988-6
ISSN: 0079-7065