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.
journal_name
Chem Pharm Bull (Tokyo)journal_title
Chemical & pharmaceutical bulletinauthors
Aoki T,Tanaka T,Watabe Hdoi
10.1248/cpb.40.1236subject
Has Abstractpub_date
1992-05-01 00:00:00pages
1236-9issue
5eissn
0009-2363issn
1347-5223journal_volume
40pub_type
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pub_type: 杂志文章
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更新日期:2015-01-01 00:00:00
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pub_type: 杂志文章
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