Purification and Characterization of γ-Enolase from Various Mammals

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The gamma subunit of enolase (γ-enolase) was purified from the brain tissues of cow, dog, goat, pig, rabbit, and rat. The purificaiton was achieved in only three steps : ammonium sulfate-precipitation, DE 53 cellulose ion-exchange chromatography, and polyacrylamide gel electrophoresis (PAGE) in a preparative mode. The purification procedure was comparatively more simple than previously reported methods, and the yield of γ-enolase was sufficient for subsequent structural and immunological analyses. In all mammals, the purified γ-enolase migrated in sodium dodecyl sulfate-PAGE (SDS-PAGE) with a molecular mass of 46 kilodaltons (kDa), and the immunological cross-reactivity between those γ-enolases was very strong. The structural homology of these γ-enolases was examined by peptide mapping using cyanogen bromide cleavage and subsequent two-dimensional electrophoresis. The resulting peptide patterns were highly similar and in cow, dog, and goat, the patterns were almost identical. These results indicate that structural homology, that is, the species non-specificity of γ-enolase, appears to be very high.
公益社団法人日本薬学会の論文
1992-05-25