Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells. |
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| Authors: | J Ku?nicki A Filipek |
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| Affiliation: | Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland. |
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| Abstract: | A novel Ca2+-binding protein (CaBP) was identified in Ehrlich-ascites-tumour cells and purified to homogeneity. The molecular mass of this protein is about 10.5 kDa as estimated by polyacrylamide-gel electrophoresis in the presence of SDS. CaBP has two Ca2+-binding sites that bind Ca2+ with a dissociation constant of about 3 x 10(-6)M. Ca2+ binding to CaBP decreases its electrophoretic mobility in urea/polyacrylamide gels, changes its u.v. spectrum, increases the intrinsic tyrosine fluorescence intensity and strengthens hydrophobic interaction with the phenyl-Sepharose matrix. |
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