Sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus, is a monomer‐tetramer associating protein

FEBS Letters

Mancheño, José M.²  Oñaderra, Mercedes²  Alfonso, Carlos¹  de los Rı́os, Vivian²  Gavilanes, José G.²  Martı́nez del Pozo, Alvaro²  Rivas, Germán¹ 

[1] Centro de Investigaciones Biológicas, CSIC, Velázquez 144, 28006 Madrid, Spain;Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Quı́mica, Universidad Complutense, 28040 Madrid, Spain

关键词: Protein cross-linking;    Sedimentation equilibrium;    Actinoporin;    BS3;    bis-(sulfosuccinimidyl) suberate;    DTSSP;    dithiobis-(sulfosuccinimidyl) propionate;    Stn-II;    Stichodactyla helianthus sticholysin II;   

DOI  :  10.1016/S0014-5793(99)00846-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sticholysin II (Stn-II) is a pore-forming cytolysin. Stn-II interacts with several supports for size exclusion chromatography, which results in an abnormal retardation precluding molecular mass calculations. Sedimentation equilibrium analysis has revealed that the protein is an associating system at neutral pH. The obtained data fit a monomer-tetramer equilibrium with an association constant K ^c ₄ of 10⁹ M⁻³. The electrophoretic pattern of Stn-II treated with different cross-linking reagents, in a wide range of protein concentrations, corroborates the existence of tetrameric forms in solution. A planar configuration of the four monomers, C4 or D2 symmetry, is proposed from modelling of the cross-linking data.

【 授权许可】

Unknown