Identification of Chaperonin Particles in Mammalian Brain Cytosol and of T-Complex Polypeptide 1 as One of Their Components
Version of Record online: 5 OCT 2006
Journal of Neurochemistry
Volume 60, Issue 6, pages 2327–2330, June 1993
How to Cite
Roobol, A. and Carden, M. J. (1993), Identification of Chaperonin Particles in Mammalian Brain Cytosol and of T-Complex Polypeptide 1 as One of Their Components. Journal of Neurochemistry, 60: 2327–2330. doi: 10.1111/j.1471-4159.1993.tb03524.x
- Issue online: 5 OCT 2006
- Version of Record online: 5 OCT 2006
- Resubmitted manuscript received February 26, 1993; accepted March 1, 1993.
- Molecular chaperone;
- Protein folding and assembly.
Abstract: An ˜950-kDa heteromeric particle was purified from guinea-pig and rat brain by sucrose gradient fractionation of post-mitochondrial supernatants. Further purification, by affinity chro-matography on ATP-Sepharose and anion exchange FPLC on MonoQ, yielded a particle with typical chaperonin ultrastructure. One of the component polypeptides was recognized by a monoclonal antibody to murine T-complex polypeptide 1. Brain cytosolic chaperonin particles formed a binary complex with unfolded tubulin subunits. The polypeptide compositions of the cytosolic chaperonin particles appeared very similar between brain and testicular tissues of the same animal, but differed subtly between the guineapig and rat.