Abstract
A protease which cleaves human immunoglobulin A1 (IgA1) has been purified from broth cultures of Neisseria gonorrhoeae. This IgA1 protease is produced by pilated and nonpilated gonococci throughout their growth cycles. A combination of ammonium sulfate precipitation, column chromatography, and either isoelectric focusing or affinity chromatography was utilized to obtain an enzyme preparation that showed approximately 3,800-fold purification and exhibited two bands (65,000 and 70,000 daltons) by analytical polyacrylamide electrophoresis in the presence of sodium dodecyl sulfate and reducing conditions. IgA1 protease activity is dependent on divalent cations and is heat labile. Detection and quantitation of IgA protease activity utilized an assay in which [125I]IgA1 is incubated with protease preparations and the cleavage products are analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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