Biophysical properties of human erythrocyte spectrin at alkaline pH: implications for spectrin structure, function, and association

Biochemistry
T FujitaM B Morris

Abstract

The effects of pH 6-13 on the conformation and assembly of spectrin were studied by means of analytical ultracentrifugation, circular dichroism (CD), 1H NMR, and UV spectrophotometry. Sedimentation velocity analysis showed that spectrin oligomers dissociate cooperatively into component alpha- and beta-subunits above pH 9.5, and that spectrin tetramers, heterodimers, and monomers adopt more extended and/or expanded shapes above this pH. The dissociation to monomers is mostly completed by pH 10.5 and is used as the basis for purifying the subunits [see Fujita et al. (1998) Biochemistry 37, 272-280]. Along with the dissociation, biphasic unfolding of spectrin was observed above pH 9.5 as detected by CD. The first phase of the transition occurred between pH 9.5 and 11, and the second phase between pH 11 and 13. A similar biphasic dependence was observed for the upfield shift of lysine epsilon-CH2 resonances detected by spin-echo 1H NMR and the spectrophotometric titration of the absorbance at 294 nm. These data indicate that deprotonation of tyrosine and lysine residues is closely correlated with (i) the dissociation of spectrin oligomers into heterodimers, (ii) the dissociation of heterodimers into monomers, and (iii) the unfoldin...Continue Reading

References

Jun 1, 1978·The Biochemical Journal·K J Ellis, R G Duggleby
May 22, 1992·Biochimica Et Biophysica Acta·N Cole, G B Ralston
Jan 1, 1993·Annual Review of Cell Biology·V Bennett, D M Gilligan

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Citations

Nov 27, 2002·Cell Motility and the Cytoskeleton·Sibnath Ray, Abhijit Chakrabarti
Feb 16, 2005·Journal of Fluorescence·Sibnath RayAbhijit Chakrabarti
Jul 25, 2019·Journal of the Royal Society, Interface·Jing CongTianzhi Luo

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