Open AccessComparative Study of the Primary Structures of Cytochrome b 5 from Four Species
Author(s) -
Akira Tsugita,
Midori Kobayashi,
Seiji Tani,
Sukei Kyo,
M. A. Rashid,
Yukuo Yoshida,
Toshimasa Kajihara,
Bunji Hagihara
Publication year - 1970
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.67.1.442
Subject(s) - cytochrome b , protein primary structure , cytochrome , cytochrome c , amino acid , biochemistry , chemistry , primary (astronomy) , biology , peptide , peptide sequence , stereochemistry , enzyme , mitochondrion , gene , phylogenetic tree , physics , astronomy
The primary structures of human, bovine, and chicken cytochromeb 5 have been determined and compared with that of the previously studied rabbit protein. One peptide containing 31 amino acid residues and another containing 10 were found common to all four species. The substitutions of amino acids between species could be accounted for mainly by single base exchange, with a few exceptional double base exchanges for the chicken. Results for bovine cytochromeb 5 differ significantly from those previously reported for calf cytochromeb 5 .