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• W1566678551 abstract "Publisher Summary The chapter presents a study on the purification of recombinant plant and animal GroES homologs focusing on chloroplast and mitochondrial chaperonin 10. The chapter describes large-scale purification schemes for spinach chloroplast cpnl0 (ch-cpnl0) and mouse mitochondrial cpnl0 (mt-cpnl0), two eukaryotic GroES homologs that are available as functional recombinant proteins. Although both proteins can be purified from their natural sources, the yields obtained are insufficient for biochemical and structural studies. In contrast, the two recombinant proteins are readily abundant and easily purified to homogeneity. Purification schemes for recombinant human and rat mt-cpnl0 are also available, and an affinity purification procedure, potentially applicable to all cpnl0 homologs, has been published. Cpn60 and cpnl0 are also both required for protein folding in these organelles. The higher plant ch-cpn10and mammalian mt-cpn10 was initially identified through their abilities to form stable, isolatable complexes with GroEL. The recombinant spinach ch-cpnl0 and mouse mt-cpnl0 are both well expressed in Escherichia coli , at levels exceeding 10% of the total soluble protein. The first step in the purification of the spinach ch-epnl0 uses the cation exchange resin S-Sepharose Fast Flow. The purified eukaryotic GroES homologs are both able to assist GroEL in the in vitro refolding of prokaryotic Rubisco." @default.
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• W1566678551 date "1998-01-01" @default.
• W1566678551 modified "2023-09-27" @default.
• W1566678551 title "[19] Purification of recombinant plant and animal GroES homologs: Chloroplast and mitochondrial chaperonin 10" @default.
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• W1566678551 doi "https://doi.org/10.1016/s0076-6879(98)90021-0" @default.
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