Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin

被引:5
作者
Morgan, PJ
Harrison, G
Freestone, PPE
Crane, D
Rowe, AJ
Mitchell, TJ
Andrew, PW
Gilbert, RJC
机构
[1] UNIV LEICESTER, DEPT BIOCHEM, NCMH, LEICESTER LE1 7RH, LEICS, ENGLAND
[2] NATL INST BIOL STAND & CONTROLS, MOL STRUCT LAB, POTTERS BAR EN6 3QG, HERTS, ENGLAND
[3] UNIV LEICESTER, DEPT IMMUNOL & MICROBIOL, LEICESTER LE1 9HN, LEICS, ENGLAND
关键词
pneumolysin; domain structure and function; analytical ultracentrifugation; electron microscopy; circular dichroism;
D O I
10.1016/S0014-5793(97)00838-7
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
Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease It creates two fragments of 37 and 15 kDa, This paper describes the purification of these two fragments and their subsequent physical and biological characterisation, The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein,,ia membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:563 / 567
页数:5
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