title: Purification and characterization of calsequestrin from chicken cerebellum.
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).
authors.affiliation: Centro di Studio per la Biologia e la Fisiopatologia Muscolare del CNR, Università di Padova, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Volpe
authors.forename: S
authors.initials: S
authors.lastname: Furlan
authors.forename: E
authors.initials: E
authors.lastname: Damiani
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002118:Calcium / Q000378:metabolism; D002155:Calsequestrin / Q000302:isolation & purification* / Q000378:metabolism; D002531:Cerebellum / Q000378:metabolism*; D002645:Chickens; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D013050:Spectrometry, Fluorescence
chemical_list: D002155:Calsequestrin; D002118:Calcium