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Bioorg Khim ; 36(1): 89-97, 2010.
Artigo em Russo | MEDLINE | ID: mdl-20386581

RESUMO

A method of the isolation and purification of IgAl protease from a culture of Neisseria meningitidis serogroup A has been developed. Three inactivated intermediates of the production of the meningococcal vaccine, a culture liquid, as well as a supernatant and sediment obtained by the precipitation of bacterial cells by cetavlon, served as a starting material. The purity of IgA1 protease was determined by SDS-PAGE. An immunoenzyme assay for determining the IgA1 protease activity has been devised. The yield of the enzyme with a specific activity of 0.5 to 4 million units/mg from 103 g of the cetavlon precipitate (40 l of culture liquid) was about 600 mug. It was shown that IgAl protease isolated from serogroup A meningococcus is capable of protecting experimental animals (mice) infected with meningococcus of serogroup B.


Assuntos
Imunoglobulina A/metabolismo , Neisseria meningitidis/enzimologia , Serina Endopeptidases/metabolismo , Animais , Meningite Meningocócica/imunologia , Meningite Meningocócica/prevenção & controle , Vacinas Meningocócicas/imunologia , Camundongos , Camundongos Endogâmicos BALB C , Neisseria meningitidis/fisiologia , Serina Endopeptidases/imunologia , Serina Endopeptidases/isolamento & purificação
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