[Isolation and determination of activity of IgA1 protease from Neisseria meningitidis].
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.
Iagudaeva
E Iu
EIu
Zhigis
L S
LS
Razguliaeva
O A
OA
Zueva
V S
VS
Mel'nikov
E E
EE
Zubov
V P
VP
Kozlov
L V
LV
Bichucher
A M
AM
Kotel'nikova
O V
OV
Alliluev
A P
AP
Avakov
A E
AE
Rumsh
L D
LD
D000818:Animals; D007070:Immunoglobulin A / Q000378:metabolism*; D008585:Meningitis, Meningococcal / Q000276:immunology / Q000517:prevention & control; D022401:Meningococcal Vaccines / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D009345:Neisseria meningitidis / Q000201:enzymology* / Q000502:physiology; D012697:Serine Endopeptidases / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*
D007070:Immunoglobulin A; D022401:Meningococcal Vaccines; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase