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• W2059522013 abstract "Enzymatically-catalyzed condensation of cytochrome c fragments, ferrous heme fragment (1-38) and apofragment (39-104), has allowed the back-conversion of cytochrome c complex to native cytochrome c. The conversion was accomplished in 90% (v/v) glycerol, a solvent which has been shown to decrease the ionization of the terminal alpha-carboxyl group liberated during hydrolysis of a peptide bond. The effect on the pK is probably the main reason the thermodynamic obstacle to re-synthesis is minimized. A 30% conversion to cytochrome c was obtained. The cytochrome c product was distinguished from the non-covalent complex and separated fragments by molecular weight analysis with sodium dodecyl sulfate polyacrylamide gel electrophoresis, by elution from Sephadex G-50 and sulfopropyl-Sephadex in the presence of denaturant, by amino acid analysis of the product purified under complex-dissociation conditions, and by spectral analysis of the absorption bands of the heme. This method provides an opportunity to study the covalent rather than the complex form of cytochrome c analogs." @default.
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• W2059522013 date "2009-01-12" @default.
• W2059522013 modified "2023-10-18" @default.
• W2059522013 title "CLOSTRIPAIN-CATALYZED RE-FORMATION OF A PEPTIDE BOND IN A CYTOCHROME C FRAGMENT COMPLEX*" @default.
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• W2059522013 doi "https://doi.org/10.1111/j.1399-3011.1981.tb02990.x" @default.
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