Purification, characterization, and comparison of the immunoglobulin A1 proteases of Neisseria gonorrhoeae.
AUTOR(ES)
Simpson, D A
RESUMO
Each isolate of Neisseria gonorrhoeae produces one of two distinct immunoglobulin A1 (IgA1) proteases, type 1 or type 2, which are known to possess different cleavage specificities for peptide bonds in the hinge region of human IgA1. Both proteases were secreted into the culture medium throughout exponential growth; however, the activity level of the type 2 protease was 10-fold that observed for the type 1 enzyme. The type 2 protease was quite stable and resistant to a variety of inhibitors. In contrast, the type 1 enzyme was highly unstable and inhibited by low concentrations of metal chelators, salts, and thiol- or serine-specific chemical reagents. Both types of gonococcal IgA1 protease were purified from broth culture supernatants by a combination of anion-exchange, chromatofocusing, and molecular sieve chromatography techniques. The stable type 2 enzyme comprised a 114-kilodalton (kDa) peptide which converted to a still active 109-kDa peptide during isolation. In contrast, the type 1 protease possessed a 112-kDa peptide which did not convert to a smaller form and which could not be dissociated from peptides of 34 and 31 kDa without complete loss of enzyme activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=211043Documentos Relacionados
- Studies on gonococcus infection. XVI. Purification of Neisseria gonorrhoeae immunoglobulin A1 protease.
- Purification and characterization of DNA methyltransferases from Neisseria gonorrhoeae.
- Molecular polymorphism and epidemiology of Neisseria meningitidis immunoglobulin A1 proteases.
- Purification and partial characterization of the major outer membrane protein of Neisseria gonorrhoeae.
- Antigenic relationships among immunoglobulin A1 proteases from Haemophilus, Neisseria, and Streptococcus species.