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.
Research Article| January 01 1989
Common epitopes of bovine lens multicatalytic-proteinase-complex subunits
B J Wagner;
Biochem J (1989) 257 (1): 265–269.
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B J Wagner, J W Margolis; Common epitopes of bovine lens multicatalytic-proteinase-complex subunits. Biochem J 1 January 1989; 257 (1): 265–269. doi: https://doi.org/10.1042/bj2570265
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