Identification of a novel calcium binding protein from bovine brain

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Abstract
A novel Ca 2+ binding protein, named caligulin, was extracted from the heat-treated 100 000 × g supernatant of bovine brain and purified to electrophoretic homogeneity. The apparent M r of caligulin determined on sodium dodecyl sulfate polyacrylamide gels was 24 000. Analysis by gel filtration chromatography indicated an apparent M r of 33 000, suggesting a monomeric protein. Amino acid composition data demonstrated the presence of 25% acidic residues, 12% basic residues and 10% leucine. In the presence of 1 mM MgCl 2 and 0.15 M KCl, caligulin bound 1 mol Ca 2+ /mol protein with half-maximal binding at about 0.2 μM Ca 2+ .