English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse
  1. View item / 
  2. Item Summary

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X-100

MPS-Authors
/persons/resource/persons255902

Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons257971

Boss,  Karin
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons256087

Dorst,  Hans-Jürgen
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons259960

Pappert,  Gunter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Schubert, D., Boss, K., Dorst, H.-J., Flossdorf, J., & Pappert, G. (1983). The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X-100. FEBS Letters, 163(1), 81-84. doi:10.1016/0014-5793(83)81168-5.


Cite as: https://hdl.handle.net/21.11116/0000-0008-4AB8-6
Abstract
Stable noncovalent dimers of band 3 protein from human erythrocyte membranes, in which state the protein is thought to exist after solubilization by the nonionic detergent Triton X-100, do not occur when purified batches of the detergent are used. Instead, the protein is in a monomer/dimer/tetramer association equilibrium. The stable dimers do appear, however, when the detergent has been 'aged'. They thus seem to be artifacts.