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

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 (St...

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Bibliographic Details
Published in:Biochemical journal 1970-03, Vol.117 (1), p.183-192
Main Authors: Thompson, E W, Laycock, M V, Ramshaw, J A, Boulter, D
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chymotrypsin
Cytochromes - analysis
Mitochondria
Peptides
Plants - analysis
Species Specificity
Triticum
Trypsin
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Summary: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 in-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 3mumol, by using chymotryptic and tryptic peptides which were analysed by the ;dansyl'-Edman method (Gray & Hartley, 1963a), with confirmation by amino acid analysis.
ISSN:0264-6021
DOI:10.1042/bj1170183