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

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.

References

Feb 20, 1979·Biochemistry·G A Homandberg, M Laskowski
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Jan 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·P J BoonR J Nivard
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Citations

Sep 1, 1982·Applied Biochemistry and Biotechnology·I M ChaikenF Widmer
Mar 1, 1990·International Journal of Peptide and Protein Research·V De Filippis, A Fontana
Jan 1, 1983·International Journal of Peptide and Protein Research·T KanmeraI M Chaiken
May 22, 2002·Protein Science : a Publication of the Protein Society·Sonati Srinivasulu, A Seetharama Acharya
Feb 15, 1996·Enzyme and Microbial Technology·I GillE N Vulfson

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