Identification of chaperonin particles in mammalian brain cytosol and of T-complex polypeptide 1 as one of their components.
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.
Roobol
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Biological Laboratory, University of Kent, Canterbury, England.
Carden
M J
MJ
D000818:Animals; D000911:Antibodies, Monoclonal; D001921:Brain / Q000378:metabolism*; D001923:Brain Chemistry; D002499:Centrifugation, Density Gradient; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000737:chemistry / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D016900:Neurofilament Proteins / Q000302:isolation & purification*; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D013737:Testis / Q000737:chemistry / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism
D000911:Antibodies, Monoclonal; D046911:Macromolecular Substances; D016900:Neurofilament Proteins; D011506:Proteins; D014404:Tubulin; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins