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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Sep;67(1):442–447. doi: 10.1073/pnas.67.1.442

Comparative Study of the Primary Structures of Cytochrome b5 from Four Species*

Akira Tsugita 1,2,, Midori Kobayashi 1,2, Seiji Tani 1,2, Sukei Kyo 1,2, M A Rashid 1,2,, Yukuo Yoshida 1,2, Toshimasa Kajihara 1,2, Bunji Hagihara 1,2
PMCID: PMC283224  PMID: 5272324

Abstract

The primary structures of human, bovine, and chicken cytochrome b5 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 cytochrome b5 differ significantly from those previously reported for calf cytochrome b5.

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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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