Purification and characterization of gamma-enolase from various mammals.

Abstract:

:The gamma subunit of enolase (gamma-enolase) was purified from the brain tissues of cow, dog, goat, pig, rabbit, and rat. The purification 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 gamma-enolase was sufficient for subsequent structural and immunological analyses. In all mammals, the purified gamma-enolase migrated in sodium dodecyl sulfate-PAGE (SDS-PAGE) with a molecular mass of 46 kilodaltons (kDa), and the immunological cross-reactivity between those gamma-enolases was very strong. The structural homology of these gamma-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 gamma-enolase, appears to be very high.

authors

Aoki T,Tanaka T,Watabe H

doi

10.1248/cpb.40.1236

subject

Has Abstract

pub_date

1992-05-01 00:00:00

pages

1236-9

issue

5

eissn

0009-2363

issn

1347-5223

journal_volume

40

pub_type

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