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A reliable system for expression and purification of the
recombinant Cyt2Aa1 toxin has been developed. The recombinant
Cyt2Aa1 toxin has been produced, characterized, followed by the
construction of the cysteine mutants V186C and L189C by site
directed mutagenesis.The hemolytic activity of the V186C mutant
exceeds that of wild type Cyt2Aa1 toxin and of the L189C
mutant.Calcein release assay experiments have been done to examine
the activity of the toxin with different artificial liposomes. It
was found that Cyt2Aa1 toxin is very active with DMPC, DMPC+DMPG
unilamellar liposomes.
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