Antibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testis.
We describe a panel of antibodies specific to individual subunits of the chaperonin-containing TCP-1 (CCT) and one antibody that reacts with all the subunits of CCT. Immunoblot analysis of CCT purified from mouse testis suggests that the testis-specific subunit, S6, may be related to CCT zeta and that a co-purifying 63 kDa protein may be a novel subunit of CCT. Using these antibodies in the analysis of CCT subjected to nondenaturing IEF we observed the resolution of two distinct conformations of CCT, which differ in their susceptibility to proteolysis and in the number of associated polypeptides.
Hynes
G
G
CRC Centre for Cell and Molecular Biology, Institute of Cancer Research, Chester Beatty Laboratories, London, UK.
Kubota
H
H
Willison
K R
KR
D000818:Animals; D000906:Antibodies / Q000276:immunology; D018833:Chaperonins / Q000737:chemistry*; D006868:Hydrolysis; D047908:Intracellular Signaling Peptides and Proteins; D008297:Male; D051379:Mice; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins / Q000737:chemistry* / Q000276:immunology; D011487:Protein Conformation; D013737:Testis / Q000737:chemistry*; D044767:Ubiquitin-Protein Ligases; D056427:t-Complex Genome Region
D000906:Antibodies; D047908:Intracellular Signaling Peptides and Proteins; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; C116196:PPP1R11 protein, human; D044767:Ubiquitin-Protein Ligases; D018833:Chaperonins