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  • Title: Purification of a novel 30,000 Da calcium-binding protein from bovine cerebellum.
    Author: Kurokawa H, Nonomura Y.
    Journal: J Biochem; 1988 Jan; 103(1):8-10. PubMed ID: 3360765.
    Abstract:
    A novel very acidic calcium-binding protein (CaBP) was purified from bovine cerebellum, using 45Ca autoradiography as a marker, through a preparative procedure involving salting out with a very high concentration of ammonium sulfate, DE52 column chromatography, RNAase treatment, and HPLC gel filtration. This protein showed a molecular weight of 30,0000 dalton (Da) on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and of 120,000 on in gel filtration chromatography analysis under physiological ionic strength. The calcium binding activity of this 30,000 Da CaBP was monitored on the basis of calcium-dependent changes in tyrosine fluorescence (Kd = 3.0 microM).
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