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Journal Article

Conformational changes of spectrin as a result of calcium binding


Rudloff,  Victor
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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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
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. 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-binding was measured by use of Ca2-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.