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

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.

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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; band 3 protein; hydrophobic protein; hydrophilic derivatives; detergent-free gel filtration and medium pressure liquid chromatography
 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.

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Language(s): eng - English
 Dates: 1983-12-272009-10-161984-05-01
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1515/bchm2.1984.365.1.525
PMID: 6469214
 Degree: -

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Title: Hoppe-Seyler's Zeitschrift für physiologische Chemie
  Abbreviation : Hoppe Seylers Z Physiol Chem
Source Genre: Journal
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Affiliations:
Publ. Info: Berlin, Germany : Walter De Gruyter
Pages: - Volume / Issue: 365 (5) Sequence Number: - Start / End Page: 525 - 530 Identifier: ISSN: 0018-4888