Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells
- 1 November 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 247 (3) , 663-667
- https://doi.org/10.1042/bj2470663
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 .times. 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 interactions with the phenyl-Sepharose matrix.This publication has 19 references indexed in Scilit:
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