Conformational changes of spectrin as a result of calcium binding

Brauer, Elfriede; Kupka, K.-D.; Rudloff, Victor

doi:10.1016/0302-4598(76)80041-4

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Conformational changes of spectrin as a result of calcium binding

MPS-Authors

/persons/resource/persons255900

Rudloff, Victor
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

Brauer, E., Kupka, K.-D., & Rudloff, V. (1976). Conformational changes of spectrin as a result of calcium binding. Bioelectrochemistry and Bioenergetics, 3(3-4), 509-518. doi:10.1016/0302-4598(76)80041-4.

Cite as: https://hdl.handle.net/21.11116/0000-0008-7006-3

Abstract

Spectrin, a protein situated at the inner surface of the red cell membrane, was investigated with respect to conformational and aggregational changes with and without Ca^2÷. The spectrin was used both as a freshly prepared sample from human blood not older than one week and as a sample extracted from deep-frozen ghosts. The aim was to determine the influences on the multiple acid base equilibria.
Ca2^2÷-binding was measured by use of Ca2^2÷-sensitive electrodes; sedimentation coefficients are directly connected to conformational changes.
The sedimentation coefficients increase with salt concentrations; even low contents of CaCl₂ cause a remarkable increase in the sedimentation velocity, whereas NaCl shows to exert only a slight effect.