Organizational differences in the membrane proteins of normal and irreversibly sickled erythrocytes

Robert W. Rubin, Clara Milikowski, Gary E. Wise

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Using two-dimensional gels, no unique membrane proteins were detected in irreversibly sickled cells. Membranes from irreversibly sickled cells were shown to cross-link much more readily with dithiobis(succinimidyl propionate) than normal erythrocyte membranes. Increased binding of band 4.5 protein and increased intra-chain disulfides were also demonstrated. These changes may correlate to enhanced cellular rigidity.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalBBA - Biomembranes
Volume595
Issue number1
DOIs
StatePublished - Jan 12 1980

Fingerprint

Membrane Proteins
Erythrocytes
Membranes
Erythrocyte Membrane
Rigidity
Disulfides
Gels
Proteins
dithiobis(succinimidylpropionate)

Keywords

  • (Lymphocyte)
  • Capping
  • Fluorescent probe
  • Ion flux
  • Potential change

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Medicine(all)

Cite this

Organizational differences in the membrane proteins of normal and irreversibly sickled erythrocytes. / Rubin, Robert W.; Milikowski, Clara; Wise, Gary E.

In: BBA - Biomembranes, Vol. 595, No. 1, 12.01.1980, p. 1-8.

Research output: Contribution to journalArticle

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