scholarly journals Changes in the structure and catalytic activities of the bovine pituitary multicatalytic proteinase complex following dialysis.

1993 ◽  
Vol 268 (3) ◽  
pp. 2029-2036
Author(s):  
B. Yu ◽  
M.E. Pereira ◽  
S. Wilk
1989 ◽  
Vol 257 (1) ◽  
pp. 265-269 ◽  
Author(s):  
B J Wagner ◽  
J W Margolis

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.


1993 ◽  
Vol 47 (4-6) ◽  
pp. 306-313 ◽  
Author(s):  
Sherwin Wilk ◽  
Maria E. Figueiredo-Pereira

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