The 240-kDa subunit of human erythrocyte spectrin binds calmodulin at micromolar calcium concentrations

The binding of the isolated α-subunit of human erythrocyte spectrin to calmodulin is demonstrated by partitioning in aqueous two-phase systems. The affinity of the α-subunit for calmodulin is slightly higher than that of the spectrin dimer, whereas the β-subunit interacts only very weakly. The bindi...

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Veröffentlicht in:	FEBS letters 1986-06, Vol.201 (2), p.306-310
Hauptverfasser:	Berglund, Åsa, Backman, Lars, Shanbhag, Vithaldas P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Calcium - pharmacology calmodulin Calmodulin - metabolism Chemical Phenomena Chemistry, Physical Chlorpromazine - pharmacology erythrocytes Fundamental and applied biological sciences. Psychology Glycoproteins Humans Macromolecular Substances man Osmolar Concentration Protein Binding - drug effects Protein Conformation Proteins spectrin Spectrin - metabolism
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Zusammenfassung:	The binding of the isolated α-subunit of human erythrocyte spectrin to calmodulin is demonstrated by partitioning in aqueous two-phase systems. The affinity of the α-subunit for calmodulin is slightly higher than that of the spectrin dimer, whereas the β-subunit interacts only very weakly. The binding is in all cases calcium-dependent and is abolished on addition of chlorpromazine. At an ionic strength close to physiological conditions, about 1 μM free calcium is required to induce maximum binding of calmodulin to spectrin dimer. Calmodulin (Human) Spectrin Erythrocyte cytoskeleton Aqueous two-phase partitioning
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(86)80629-9