PMID: 6273349Oct 1, 1981Paper

Clostripain-catalyzed re-formation of a peptide bond in a cytochrome C fragment complex

International Journal of Peptide and Protein Research
M A Juillerat, G A Homandberg


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.


Feb 20, 1979·Biochemistry·G A Homandberg, M Laskowski
Feb 5, 1976·Journal of Molecular Biology·R E DickersonR J Almassy
Jan 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·P J BoonR J Nivard
Jun 19, 1979·Biochimica Et Biophysica Acta·P T Nix, P K Warme
Aug 28, 1979·Biochemical and Biophysical Research Communications·A K KoulP K Warme
Dec 23, 1974·Biochemical and Biophysical Research Communications·G Corradin, H A Harbury
Mar 19, 1971·Biochemical and Biophysical Research Communications·B R Sreenathan, C P Taylor
Dec 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·G Corradin, H A Harbury
Jan 1, 1967·Biochemistry·M S Doscher, C H Hirs
Nov 1, 1980·International Journal of Peptide and Protein Research·A KomoriyaI M Chaiken

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