Isolation and determination of activity of IgA1 protease from Neisseria meningitidis

• Published in: Bioorganicheskaia khimiia Vol. 36; no. 1; p. 89
• Main Authors: Iagudaeva, E Iu, Zhigis, L S, Razguliaeva, O A, Zueva, V S, Mel'nikov, E E, Zubov, V P, Kozlov, L V, Bichucher, A M, Kotel'nikova, O V, Alliluev, A P, Avakov, A E, Rumsh, L D
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01.01.2010
• Subjects: Animals; Immunoglobulin A - metabolism; Meningitis, Meningococcal - immunology; Meningitis, Meningococcal - prevention & control; Meningococcal Vaccines - immunology; Mice; Mice, Inbred BALB C; Neisseria meningitidis - enzymology; Neisseria meningitidis - physiology; Serine Endopeptidases - immunology; Serine Endopeptidases - isolation & purification; Serine Endopeptidases - metabolism
• ISSN: 0132-3423

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.