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

被引：52

作者：

de los Ríos, V

Mancheño, JM

del Pozo, AM

Alfonso, C

Rivas, G

Oñaderra, M

Gavilanes, JG ^{[1
]}

机构：

[1] Univ Complutense Madrid, Fac Quim, Dept Bioquim & Biol Mol, E-28040 Madrid, Spain

[2] CSIC, Ctr Invest Biol, E-28006 Madrid, Spain

来源：

FEBS LETTERS | 1999年 / 455卷 / 1-2期

关键词：

protein cross-linking; sedimentation equilibrium; actinoporin;

D O I：

10.1016/S0014-5793(99)00846-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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-4(c) Of 10(9) M-3. The electrophoretic pattern of Stn-II treated with different crosslinking 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. (C) 1999 Federation of European Biochemical Societies.

引用

页码：27 / 30

页数：4

共 33 条

[1] Phage empty set 29 protein p6 is in a monomer-dimer equilibrium that shifts to higher association states at the millimolar concentrations found in vivo [J].