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- W1531018587 abstract "Publisher Summary The chapter presents a study on the purification of yeast mitochondrial chaperonin 60 and co-chaperonin 10. The chapter describes a large-scale purification procedure of S. cerevisiae hsp60 expressed in Pichia pastoris. Yeast cpnl0 was isolated by taking advantage of the fact that bacterial GroEL forms a functional complex with co-chaperonins from mitochondria or chloroplasts. Chaperonin system is not involved in the folding of all mitochondrial proteins. Assaying the interaction of purified hsp60 and cpnl 0 with authentic substrate proteins should give insight into the specificity of the mitochondrial chaperonin system. In addition, a comparison of the bacterial GroEL/ES system with the eukaryotic hsp60/cpnl0 system may help to elucidate the chaperonin reaction cycle. The chapter describes the procedure for purification of recombinant heat shock protein 60, purification of recombinant authentic and hexahistidine-tagged chaperonin 10, and also mentions the characterization of purified yeast chaperonins." @default.
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- W1531018587 date "1998-01-01" @default.
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- W1531018587 title "[17] Purification of yeast mitochondrial chaperonin 60 and co-chaperonin 10" @default.
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- W1531018587 doi "https://doi.org/10.1016/s0076-6879(98)90019-2" @default.
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