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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 Ca2÷. 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.
Ca22÷-binding was measured by use of Ca22÷-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.
