Purification and characterization of calsequestrin from chicken cerebellum |
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Authors: | P Volpe S Furlan E Damiani |
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Institution: | Centro di Studio per la Biologia e la Fisiopatologia Muscolare del CNR, Università di Padova, Italy. |
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Abstract: | 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). |
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