Purification and characterization of calsequestrin from chicken cerebellum

Chicken cerebellum microsomal fractions contain a protein tentatively identified as calsequestrin (CS) (Volpe et al., Neuron 5, 713-721, 1990). Here we report, for the first time, the purification of cerebellum CS from whole tissue homogenate by DEAE-Cellulose chromatography and Ca(2+)-dependent elution from phenyl-Sepharose. The purified cerebellum CS displays the shift and increase in intrinsic fluorescence characteristic of skeletal muscle CS, and is shown to be a high-capacity, low-affinity Ca2+ binding protein (Kd = 1 mM).