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. 1970 Mar;117(1):183–192. doi: 10.1042/bj1170183

The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c

E W Thompson 1, M V Laycock 1,*, J A M Ramshaw 1, D Boulter 1
PMCID: PMC1178845  PMID: 5420954

Abstract

The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c has been determined. The molecule consists of a single polypeptide chain of 111 amino acid residues and is homologous with other mitochondrial cytochromes c. Comparison with the amino acid sequence of wheat-germ cytochrome c (Stevens, Glazer & Smith, 1967) shows 14 differences. On alignment with mammalian cytochromes c, mung-bean cytochrome c has an N-acetylated `tail' of eight amino acid residues similar to that found in wheat-germ cytochrome c. Of the 22 positions in wheat-germ cytochrome c that contain amino acid residues unique to these positions, 20 were found to contain the same ones in mung-bean cytochrome c. The ∈-N-trimethyl-lysine residues reported for wheat-germ cytochrome c (Delange, Glazer & Smith, 1969) in positions 72 and 86 were also found in these positions in mung-bean cytochrome c. The sequence was determined from 3μmol, by using chymotryptic and tryptic peptides which were analysed by the `dansyl'–Edman method (Gray & Hartley, 1963a), with confirmation by amino acid analysis.

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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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