Abstract
When initially isolated with heme reconstitution, recombinant cytochrome c peroxidase molecules exhibit a conformation, revealed by visible spectra which observably differ from the corresponding holo proteins isolated from yeast. Binding yeast iso-1 cytochrome c to these recombinant cytochrome c peroxidases (either in solution or via an affinity column) catalyses a local refolding of the recombinant proteins to a form that is indistinguishable from the native (yeast) protein.
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