Antigenicity of proteinases from Streptomyces griseus (pronase).
The five pronase fractions, A(1), A(2), B, C (trypsin-like), and D (elastolytic), obtained by ion-exchange chromatography, were found to be antigenically distinct. Antibodies to pronase inhibited the enzymic activity of each of the enzyme fractions. Pronase trypsin and bovine trypsin, although resembling each other in enzymic activity and in amino acid sequence around their active sites, did not cross-react antigenically with, nor was their enzymic activity inhibited by, the respective homologous antibodies. Inactivation of pronase trypsin by complexing with soya-bean inhibitor AA, was not associated with a decrease in capacity to precipitate with its antibody. It is assumed that the antigenic sites are located far enough from the catalytic site of the enzyme to allow it to precipitate immunologically even when the catalytic site was blocked.
D000595:Amino Acid Sequence; D000818:Animals; D000941:Antigens / Q000032:analysis*; D001665:Binding Sites; D002417:Cattle; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D007106:Immune Sera; D005779:Immunodiffusion; D010447:Peptide Hydrolases / Q000032:analysis*; D011233:Precipitin Tests; D011480:Protease Inhibitors; D011817:Rabbits; D013025:Glycine max; D013302:Streptomyces / Q000276:immunology*; D014357:Trypsin; D014361:Trypsin Inhibitors
D000941:Antigens; D007106:Immune Sera; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D010447:Peptide Hydrolases; D014357:Trypsin