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. 1984 Feb 1;217(3):595–599. doi: 10.1042/bj2170595

The effect of complete or specific partial acetimidylation on the biological properties of cytochrome c and cytochrome c-T.

C J Wallace
PMCID: PMC1153258  PMID: 6324739

Abstract

The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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