Reoxidation and renaturation studies on the main toxin of Naja naja samarensis

FEBS Letters

Gacond, J.J.¹  Juillerat, M.A.¹  Bargetzi, J.P.¹ 

[1] Département de Biochemie, Université de Genéve, 30 Quai Ernest Ansermet, CH 1211 Genève, Switzerland

关键词: Folding;    Renaturation;    Intermediate;    Disulfide exchange;    Toxin;    Snake venom;    NT;    Naja naja samarensis;    main toxin;    n-NT;    native-like toxin;    d-NT;    denatured toxin;    HPLC;    high-performance liquid chromatography;    TEA;    triethy lamine;    TFA;    trifluoroacetic acid;    Gu-HCl;    guanidine hydrochloride;    GSH;    reduced glutathione;    GSSG;    oxidized glutathione;    DTT;    dithiothreitol;    CM-Cys;    carboxymethylcysteine;   

DOI  :  10.1016/0014-5793(84)81252-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown