Purification and spectral studies on the Ca2+-binding properties of 67 kDa calcimedin.

Abstract

The 67 kDa calcimedin, isolated by using a phenyl-Sepharose affinity column followed by DEAE-cellulose and gel-filtration chromatographies, was homogeneous by the criterion of SDS/polyacrylamide-gel electrophoresis. In non-SDS gels, the protein moved faster in the presence of EDTA, suggesting that Ca2+ binding affects its mobility in a manner similar to… (More)

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@article{Mani1989PurificationAS, title={Purification and spectral studies on the Ca2+-binding properties of 67 kDa calcimedin.}, author={Rajam S. Mani and Cyril M. Kay}, journal={The Biochemical journal}, year={1989}, volume={259 3}, pages={799-804} }