Studies on the gonococcal IgA1 protease II. Improved methods of enzyme purification and production of monoclonal antibodies to the enzyme.
Two types of extremely active proteases that cleave human IgA1 are produced by pathogenic Neisseria in minute concentrations. To study the antigenicity of these enzymes, a simplified method is described to purify these enzymes from large batch cultures to obtain a sufficient quantity of these IgA1 proteases to study these characteristics. In addition, we describe the production of both rabbit polyclonal and mouse monoclonal antibodies to one of these enzymes. One such monoclonal antibody seemed directed toward the active site of the IgA1 protease and inhibited its enzymatic activity.
Blake
M S
MS
Laboratory of Bacteriology and Immunology, Rockefeller University, New York, NY 10021.
Eastby
C
C
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis*; D004797:Enzyme-Linked Immunosorbent Assay; D051379:Mice; D008807:Mice, Inbred BALB C; D009344:Neisseria gonorrhoeae / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000276:immunology / Q000302:isolation & purification*; D011817:Rabbits; D012697:Serine Endopeptidases
D000911:Antibodies, Monoclonal; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase