Author's Organization：Department of Environmental Biochemistry, Shizuoka College of Pharmacy Department of Environmental Biochemistry, Shizuoka College of Pharmacy
The molecular weight of calcium-binding protein (CaBP) purified from the soluble fraction of normal rat liver was estimated to be 28800 by calibrated gel filtration on Sephadex G-100. Amino acid analysis of the CaBP showed glycine and glutamic acid to be the predominant amino acids. The calcium binding constant was found to be 4.19×105M-1 by equilibrium dialysis, and there appear to be 6-7 high affinity binding sites for calcium per molecule of protein.
