Monoclonal antibodies as probes for the changes in antigenicity of bovine and porcine aspartyl proteases with pH.
Two monoclonal antibodies, 918(4) and 139(7), directed against either bovine or porcine pepsin, respectively, were retained among 365 positive hybridoma clones. These monoclonal antibodies were characterized by using both indirect and sandwich ELISA. Characterization of these monoclonal antibodies was further performed by the biospecific interaction analysis (BIA-core analysis). Then, they were used as antigenic probes to study the changes in antigenicity of both bovine and porcine pepsins induced by pH. The results demonstrated the importance of the conformational change in both catalytic activities and antigenic determinant accessibility of bovine and porcine pepsins. Furthermore, our results suggest that changes in the conformation due to pH can be detected by specific monoclonal antibodies.
Boudjellab
N
N
Station de Recherche en Technologie et Analyses Laitières, Champ de Mars, Poligny Cedex, France.
Grosclaude
J
J
Zhao
X
X
Collin
J C
JC
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000276:immunology; D000918:Antibody Specificity; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000276:immunology*; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D006825:Hybridomas; D006863:Hydrogen-Ion Concentration; D008968:Molecular Conformation; D010434:Pepsin A / Q000737:chemistry* / Q000276:immunology; D013552:Swine
D000911:Antibodies, Monoclonal; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A