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Identification of Chaperonin Particles in Mammalian Brain Cytosol and of T‐Complex Polypeptide 1 as One of Their Components
Author(s) -
Roobol Anne,
Carden Martin J.
Publication year - 1993
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1993.tb03524.x
Subject(s) - fast protein liquid chromatography , chaperonin , cytosol , biochemistry , biology , cell fractionation , guinea pig , mitochondrion , microbiology and biotechnology , protein folding , enzyme , endocrinology
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.