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Identification of a novel calcium binding protein from bovine brain
Author(s) -
Morton Waisman David,
Muranyi Judith,
Mohammed Ahmed
Publication year - 1983
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(83)80023-4
Subject(s) - chemistry , size exclusion chromatography , sodium , calcium , sodium dodecyl sulfate , monomer , chromatography , leucine , mole , polyacrylamide gel electrophoresis , biochemistry , gel electrophoresis , amino acid , organic chemistry , enzyme , polymer
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+ .