Isolation and biological properties of a rabbit antibody to porcine pancreatic elastase and its use as ligand for elastase purification.
By affinity chromatography on porcine pancreatic elastase bound to Sepharose an anti-elastase antibody was isolated from the serum of rabbits who had been injected with porcine pancreatic elastase and fed a light cholesterol diet. The protein (molecular weight 150,000 daltons) was recovered with both a high degree of purity and intact biological properties. It specifically inhibited elastolysis by a mechanism distinct from that known elastase inhibition by alpha 1 antiprotease and alpha 2 macroglobulin. Results of this study indicate that inhibition is due to an IgG antibody to the porcine elastase. The antigen-antibody reaction appears to involve the active site of elastase. The isolated IgG in turn binds to activated Sepharose and the resulting immunoadsorbent system allows purification of pancreatic elastase by affinity chromatography.
D000818:Animals; D000906:Antibodies / Q000302:isolation & purification; D000937:Antigen-Antibody Reactions; D002846:Chromatography, Affinity; D005779:Immunodiffusion; D008024:Ligands; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D013552:Swine; D014357:Trypsin
D000906:Antibodies; D008024:Ligands; D010196:Pancreatic Elastase; D014357:Trypsin