Expression of the pneumolysin gene in Escherichia coli: rapid purification and biological properties.
作者信息
Mitchell T J, Walker J A, Saunders F K, Andrew P W, Boulnois G J
机构信息
Department of Microbiology, University of Leicester, U.K.
出版信息
Biochim Biophys Acta. 1989 Jan 23;1007(1):67-72. doi: 10.1016/0167-4781(89)90131-0.
PMID:2642385
Abstract
The gene for pneumolysin, the thiol-activated toxin from Streptococcus pneumoniae, has been expressed in Escherichia coli. The recombinant protein has been purified using a rapid, high yield, purification procedure and has been shown to be identical with respect to N-terminal amino-acid sequence, specific activity, effect on human polymorphonuclear phagocytes and effect on human complement to the native toxin purified from the pneumococcus. This provides a large enough source of material to begin investigation of pneumolysin as a candidate for inclusion in a pneumococcal vaccine.
摘要
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