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Calmodulin binding to human spectrin
Author(s) -
Berglund Åsa,
Backman Lars,
Shanbhag Vithaldas P.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80884-4
Subject(s) - calmodulin , spectrin , egta , chemistry , calcium , sepharose , partition coefficient , affinity chromatography , elution , partition (number theory) , chromatography , biochemistry , biophysics , biology , cytoskeleton , organic chemistry , enzyme , mathematics , combinatorics , cell
Calmodulin is shown to interact with human spectrin dimer. The binding was highly calcium‐dependent and observed in two different kinds of experiments. Firstly, affinity chromatography of calmodulin on a Sepharose 4B column with immobilized spectrin, and secondly, partition in aqueous two‐phase polymer systems. In the column experiments stoichiometric amounts of calmodulin were retained on the spectrin‐Sepharose column when micromolar concentrations of calcium were present. The calmodulin bound could be eluted with EGTA. The partition coefficient of calmodulin in an aqueous two‐phase polymer system containing calcium was changed upon addition of spectrin, indicating an association between the two proteins. In the absence of calcium, spectrin did not cause any change in the partition behaviour of calmodulin, thus showing that the association requires calcium.