Identification of a novel calcium binding protein from bovine brain

David Morton Waisman, Judith Muranyi, Ahmed Mohammed

Résultat de recherche: Articleexamen par les pairs

23 Citations (Scopus)

Résumé

A novel Ca2+ binding protein, named caligulin, was extracted from the heat-treated 100 000 × g supernatant of bovine brain and purified to electrophoretic homogeneity. The apparent Mr of caligulin determined on sodium dodecyl sulfate polyacrylamide gels was 24 000. Analysis by gel filtration chromatography indicated an apparent Mr 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 MgCl2 and 0.15 M KCl, caligulin bound 1 mol Ca2+/mol protein with half-maximal binding at about 0.2 μM Ca2+.

Langue d'origineEnglish
Pages (de-à)80-84
Nombre de pages5
JournalFEBS Letters
Volume164
Numéro de publication1
DOI
Statut de publicationPublished - nov. 28 1983
Publié à l'externeOui

Note bibliographique

Funding Information:
This work is supportedb y a Medical Research Council Operating Grant and by an Alberta Heritage Foundation for Medical Research EstablishmentG rant.

ASJC Scopus Subject Areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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