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Disulfide isomers of alpha-neurotoxins from King cobra (Ophiophagus hannah) venom.

Abstract：

:Two novel alpha-neurotoxins, Oh-6A and Oh-6B, isolated from the king cobra (Ophiophagus hannah) venom, consist of 70 amino acid residues with 10 cysteine residues and share the same amino acid sequences as determined by Edman degradation on the peptide fragments generated from the proteolytic hydrolysates. Their sequences share 46-53% homology with Oh-4, Oh-5, Toxin a, and Toxin b from the same venom. The finding that Oh-6A and Oh-6B had different retention times in the reversed-phase column suggested that the two toxin molecules should not have the same conformation. Selective reduction on the disulfide bond, Cys26--Cys30, at the tip of their loop II structures resulted in the production of the partially reduced derivatives eluted at the same position. Under redox conditions, the partially reduced Oh-6A and 6B exclusively converted into native Oh-6A as evidenced by HPLC analyses. This suggests that Oh-6A and Oh-6B are disulfide isomers which probably arise from cis-trans isomerization of the Cys26--Cys30 disulfide bond. Alternatively, the two toxins exhibited binding activity toward nAChR and lethal toxicity equally. It reflects that the diversity around the extra loop at the loop II structure does not exert a significant effect on the manifestation of the neurotoxicity of Oh-6A and Oh-6B.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lin SR,Chang LS,Chang CC

doi

10.1006/bbrc.1998.9888

subject

Has Abstract

pub_date

1999-01-08 00:00:00

pages

104-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)99888-6

journal_volume

254

pub_type

杂志文章

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