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On the anomalous behaviour on gel-filtration and SDS-electrophoresis of prothymosin-alpha.

Authors
  • Cordero, O J
  • Sarandeses, C S
  • Lopez, J L
  • Nogueira, M
Type
Published Article
Journal
Biochemistry international
Publication Date
Dec 01, 1992
Volume
28
Issue
6
Pages
1117–1124
Identifiers
PMID: 1290467
Source
Medline
License
Unknown

Abstract

The regulator of T-cell proliferation prothymosin alpha, is a protein with a relative molecular mass of 12 KDa as calculated from its amino acid sequence. This immunoregulator exhibits anomalous behaviour on gel-filtration and SDS-PAGE electrophoresis appearing as oligomers which are 5 or 2 fold larger than the corresponding polypeptide. These results suggest that a dimeric form of prothymosin alpha is stable to dissociation by SDS and reduction by beta-mercapto ethanol.

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