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

作者信息

Roobol A, Carden M J

机构信息

Biological Laboratory, University of Kent, Canterbury, England.

出版信息

J Neurochem. 1993 Jun;60(6):2327-30. doi: 10.1111/j.1471-4159.1993.tb03524.x.

DOI:10.1111/j.1471-4159.1993.tb03524.x
PMID:8098357
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.

摘要

相似文献

1
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