Isolation of neuronal parvalbumin by high-performance liquid chromatography. Characterization and comparison with muscle parvalbumin

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Abstract
Neuronal parvalbumin was isolated from rat brain and purified to homogeneity by high-performance liquid chromatography (HPLC) on reverse-phase supports. This procedure includes 4 consecutive chromatographic steps with an overall protein recovery of 74% and a 26,400-fold purification. The concentration of parvalbumin was .apprx. 10 mg/kg wt wt in brain tissue, which is about 100 times lower than that in rat muscle. The physical properties of brain parvalbumin are described and compared with those of the muscle counterpart. These proteins were identical in their MW (12,000), isoelectric points (4.9), retention times on C-18 reverse-phase HPLC columns, Ca2+ content (2/molecule), amino acid compositions, and immunological properties. A comparison of the tryptic peptide maps of brain and muscle parvalbumin by analytical HPLC also revealed identity and showed that the isolation method described here did not alter the chemical structure of the protein.