Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells.
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.
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
J
J
Kuźnicki
A
A
Filipek
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D017317:Annexin A6; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000302:isolation & purification; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D009363:Neoplasm Proteins / Q000302:isolation & purification; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D000596:Amino Acids; D017317:Annexin A6; D002135:Calcium-Binding Proteins; D009363:Neoplasm Proteins; D002118:Calcium