The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation.
作者： M E Goldberg , G Orsini
DOI: 10.1016/S0021-9258(17)34821-4
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摘要: The refolding and reoxidation of fully reduced denatured chymotrypsinogen A have been studied in the presence low concentrations guanidine HCl or urea. Renaturation yields 60 to 70% were observed when was facilitated by mixtures oxidized glutathione. Refolding occurred within a narrow range denaturant concentration (1.0 1.3 M 2 urea) which native protein shown be stable, regain correct disulfide pairing. Renatured is indistinguishable from zymogen chromatographic behavior, potential chymotryptic activity, sedimentation coefficient, spectral properties. kinetics renaturation determined. Some species obtained at various times characterized as incorrectly molecules could renatured thiol-catalyzed interchange bonds.
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