The use of monoclonal antibodies to distinguish several chemically modified forms of human alpha 1-proteinase inhibitor.
The purpose of our investigation was to obtain monoclonal antibodies that could distinguish three forms of alpha 1-proteinase inhibitor (alpha 1-PI): native alpha 1-PI, N-chlorosuccinimide-oxidized alpha 1-PI (Ox-alpha 1-PI) and proteolytically modified alpha 1-PI (alpha 1-PI). Three specific monoclonal antibodies were characterized as to their binding properties. By using the Bio-Dot assay, it was found that all three forms of alpha 1-PI were capable of binding to antibody 6D4-6-18, that only Ox-alpha 1-PI, but not native alpha 1-PI or alpha 1-PI, could bind to antibody 6C7-5, and that alpha 1-PI and a complex between alpha 1-PI and trypsin uniquely were not able to bind to antibody 5C12-8-7. Thus it was concluded that it is possible to use monoclonal antibodies with different epitopic specificities to distinguish two chemically modified forms of alpha 1-PI from the native protein.
D000911:Antibodies, Monoclonal; D000915:Antibody Affinity; D001667:Binding, Competitive; D001798:Blood Proteins / Q000276:immunology*; D000939:Epitopes / Q000276:immunology; D006801:Humans; D010084:Oxidation-Reduction; D011480:Protease Inhibitors / Q000276:immunology*; D000515:alpha 1-Antitrypsin
D000911:Antibodies, Monoclonal; D001798:Blood Proteins; D000939:Epitopes; D011480:Protease Inhibitors; D000515:alpha 1-Antitrypsin