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Reoxidation and renaturation studies on the main toxin ofNaja naja samarensis

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
178
Issue
1
Identifiers
DOI: 10.1016/0014-5793(84)81252-1
Keywords
  • Folding
  • Renaturation
  • Intermediate
  • Disulfide Exchange
  • Toxin
  • Snake Venom
Disciplines
  • Biology

Abstract

Abstract The main toxin of Naja naja samarensis is a very small and rigid protein ( M, 6850, 8 cysteines). When fully reduced, it regains its native conformation by a mechanism involving a rapid cysteine oxidation and a slower, less temperature-dependent disulfide exchange. In a native-like form of the protein we observed a population whose cysteines were incompletely reoxidized. When intermediates with blocked cysteines were incubated with oxidized and reduced glutathione, the percentage of native-like molecules increased. These findings suggest a multiple folding pathway.

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