Common epitopes of bovine lens multicatalytic-proteinase-complex subunits.
Component polypeptides of both the bovine lens and pituitary multicatalytic proteinase complexes demonstrate different immunoreactivities with a polyclonal antiserum raised against the purified pituitary enzyme. Four (Mr 24000, 26000, 34000 and 38000) of eight bands that have been resolved by SDS/polyacrylamide-gel electrophoresis are stained in immunoblot experiments. Monospecific antibodies obtained from this antiserum by affinity purification from the 38000- and 34000-Mr bands of the lens enzyme bound equally well to either band, but showed little or no binding to the 26000- and 24000-Mr bands upon immunoblotting. Antibody affinity-purified from the 24000-Mr band showed comparable binding to the 24000-, 34000- or 38000-Mr band. One explanation of these results is that the 24000-Mr polypeptide is derived from the higher-Mr polypeptide(s) and has lost some of the common immunodeterminants.
Wagner
B J
BJ
Department of Biochemistry, University of Medicine and Dentistry of New Jersey-New Jersey Medical School, Newark 07103.
Margolis
J W
JW
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002417:Cattle; D003546:Cysteine Endopeptidases / Q000276:immunology*; D000939:Epitopes / Q000032:analysis*; D015151:Immunoblotting; D007908:Lens, Crystalline / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000276:immunology*; D046988:Proteasome Endopeptidase Complex
D000911:Antibodies, Monoclonal; D000939:Epitopes; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex