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 language | English (US) |
|---|---|
| Pages (from-to) | 1-8 |
| Number of pages | 8 |
| Journal | BBA - Biomembranes |
| Volume | 595 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 12 1980 |
Keywords
- (Lymphocyte)
- Capping
- Fluorescent probe
- Ion flux
- Potential change
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Medicine(all)
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Cite this
Rubin, R. W., Milikowski, C., & Wise, G. E. (1980). Organizational differences in the membrane proteins of normal and irreversibly sickled erythrocytes. BBA - Biomembranes, 595(1), 1-8. https://doi.org/10.1016/0005-2736(80)90241-2