Identification of chaperonin particles in mammalian brain cytosol and of T-complex polypeptide 1 as one of their components.

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 (6). pp. 2327-2330. ISSN 0022-3042. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1111/j.1471-4159.1993.tb03524...

Abstract

An approximately 950-kDa heteromeric particle was purified from guinea-pig and rat brain by sucrose gradient fractionation of post-mitochondrial supernatants. Further purification, by affinity chromatography 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 guinea-pig and rat.

Item Type: Article
Projects: [122] (Wellcome Trust: grant 035 101/2/92/2/1 S).
Uncontrolled keywords: Molecular Chaperone; Protein Folding and Assembly
Subjects: Q Science
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
R Medicine
Q Science > QH Natural history > QH301 Biology
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Martin Carden
Date Deposited: 02 Oct 2009 17:21
Last Modified: 02 Oct 2009 17:21
Resource URI: http://kar.kent.ac.uk/id/eprint/22832 (The current URI for this page, for reference purposes)
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