The primary sequence of chicken myoglobin (Gallus gallus)

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

doi:10.1016/0005-2795(75)90300-1

Cited by 28 publications

(7 citation statements)

References 25 publications

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“…In addition, our results demonstrated that the molecular mass of turkey myoglobin was 300-350 Da greater than those of other well-characterized red meat myoglobins such as pig, sheep, water buffalo, horse, yak, and red deer (Table 1), which ranged from 16,911 to 17,023 Da. However, the observed molecular mass of turkey Mb was similar to that of other avian myoglobins, such as chicken (17,291 Da; Deconinck et al, 1975), spot-billed duck (17,266 Da;Miyazaki, Uchida, & Tsugita, 1998), emperor penguin (17,471 Da;Tamburrini, Romano, Giardina, & di Prisco, 1999), and ostrich (17,297 Da;Enoki, Ohga, Ishidate, & Morimoto, 2008).…”

Section: Maldi-tof Msmentioning

confidence: 68%

“…However, the number of amino acids in wellcharacterized avian myoglobins, such as chicken (Deconinck et al, 1975), spot-billed duck (Miyazaki et al, 1998), emperor penguin (Tamburrini et al, 1999), and ostrich (Enoki et al, 2008) is 153, similar to that in red meat myoglobins (www.expasy.org). This insinuated that turkey Mb may also have the same number of amino acids (153) and the possibility of the presence of large-sized amino acids in its primary structure.…”

Section: Discussionmentioning

confidence: 97%

See 1 more Smart Citation

Mass spectrometric characterization and thermostability of turkey myoglobin

Joseph

Suman

et al. 2010

LWT - Food Science and Technology

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Section: Maldi-tof Msmentioning

confidence: 68%

Section: Discussionmentioning

confidence: 97%

Mass spectrometric characterization and thermostability of turkey myoglobin

Joseph

Suman

et al. 2010

LWT - Food Science and Technology

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“…The species compared were human (Romero-Herrera and Lehmann 1974c), chimpanzee (Romero-Herrera and Lehmann 1972a), gibbon (Romero-Herrera and Lehmann 1971), baboon and macaque (Romero-Herrera and Lehmann 1972b), treeshrew (Romero-Herrera and Lehmann 1974b), marmoset, woolly monkey and squirrel monkey (Romero-Herrera and Lehmann 1973a), potto (Romero-Herrera and Lehmann 1975), lemur and galago Lehmann 1973b), badger (Tetaert et al 1974), horse (Dautrevaux et al 1969), sheep (Han et al 1972), ox (Han et al 1970), porpoise and harbour seal (Bradshaw and Gurd 1969), dolphin (Kluh and Bakaradjieva 1971), sperm whale (Edmundson 1965), kangaroo and chicken (Deconinck et al 1975).…”

Section: Estimation Of Dates Of Divergencementioning

confidence: 99%

Studies on Monotreme Proteins VII. Amino Acid Sequence of Myoglobin From the Platypus, Ornithorhynchus Anatinus

Wk¹,

Eo²

1976

Aust. Jnl. Of Bio. Sci.

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Myoglobin isolated from skeletal. muscle of the platypus contains 153 amino acid residues. lhe complete amino acid sequence has been determined following cleavage with cyanogen bromide and further digestion of the four fragments with trypsin, chymotrypsin, pepsin and thermolysin. Sequences of the purified peptides were determined by the dansyl-Edman procedure. The amino acid sequence showed 25 differences from human myoglobin and 24 from kangaroo myoglobin. Amino acid sequences in myoglobins are more conserved than sequences in the exand fi-globin chains, and platypus myoglobin shows a similar number of variations in sequence to kangaroo myoglobin when compared with myoglobin of other species. The date of divergence of the platypus from other mammals was estimated at 102 � 31 million years, based on the number of amino acid differences between species and allowing for multiple mutations during the evolutionary period. This estimate differs widely from the estimate given by similar treatment of the ex- and fi-chain sequences and a constant rate of mutation .of globin chains is not supported.

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“…In the post-genomic era, the amino acid sequences of myoglobins from several mammalian (Dosi et al, 2006;Joseph et al, 2010b;Suman, Joseph, Li, Steinke, & Fontaine, 2009) and avian (Enoki, Ohga, Ishidate, & Morimoto, 2008;Suman et al, 2010) (Deconinck et al, 1975). However, turkey myoglobin's primary structure has not been characterised.…”

Section: Introductionmentioning

confidence: 98%