ANTIBODY CHARACTERIZATION OF 2 DISTINCT CONFORMATIONS OF THE CHAPERONIN-CONTAINING TCP-1 FROM MOUSE TESTIS

We describe a panel of antibodies specific to individual subunits of t he chaperonin-containing TCP-1 (CCT) and one antibody that reacts with all the subunits of CCT. Immunoblot analysis of CCT purified from mou se testis suggests that the testis-specific subunit, S6, may be relate d to CCT zeta and that a co-purifying 63 kDa protein may be a novel su bunit of CCT. Using these antibodies in the analysis of CCT subjected to nondenaturing IEF we observed the resolution of two distinct confor mations of CCT, which differ in their susceptibility to proteolysis an d in the number of associated polypeptides.