Penguin (<i>Aptenodytes forsteri</i>) myoglobin. A 70 residue N‐terminal sequence

Peiffer, S; Deconinck, Marc Melchior; Paul, C.; Depreter, J; Ag, Schnek; Léonis, J

doi:10.1016/0014-5793(73)80481-8

FEBS Letters

1973

DOI: 10.1016/0014-5793(73)80481-8

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Penguin (Aptenodytes forsteri) myoglobin. A 70 residue N‐terminal sequence

S Peiffer

Marc Melchior Deconinck

C. Paul

et al.

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Cited by 9 publications

References 13 publications

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Evolution of myoglobin

Suzuki

Imai

1998

CMLS, Cell. Mol. Life Sci.

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The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the structures of these proteins suggests that there may be three distinct origins: a 'universal globin', a 'compact globin' and an 'IDO-like globin'.

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Evolution of myoglobin

Suzuki

Imai

1998

CMLS, Cell. Mol. Life Sci.

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The primary sequence of chicken myoglobin (Gallus gallus)

Deconinck

Peiffer

Depreter

et al. 1975

Biochimica et Biophysica Acta (BBA) - Protein Structure

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The covalent structure of dog myoglobin

Dumur

Dautrevaux

Han

1976

Biochimica et Biophysica Acta (BBA) - Protein Structure

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Penguin (Aptenodytes forsteri) myoglobin. A 70 residue N‐terminal sequence

Cited by 9 publications

References 13 publications

Evolution of myoglobin

Evolution of myoglobin

The primary sequence of chicken myoglobin (Gallus gallus)

The covalent structure of dog myoglobin

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