Primary structure of <i>N</i>‐terminal part of molecule of dolphin myoglobin

Kluh, I.; Bakardjieva, A.

doi:10.1016/0014-5793(71)80556-2

Cited by 30 publications

(11 citation statements)

References 10 publications

(4 reference statements)

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“…The primary structure of this myoglobin proved identical with that from the Atlantic bottlenosed dolphin, Tursiops truncatus, but showed four substitutions with respect to the sequence reported for the Black Sea dolphin which has also been given the designation Delphinus delphis. tryptophan residues (Fontana, 1972) to produce a long peptide to assist in confirming some amino acid substitutions found between this protein and that from the same named species from the Black Sea (Kluh and Bakardjieva, 1971). Other Cetacean myoglobin sequences reported include common porpoise (Bradshaw and Gurd, 1969) and sperm whale (Edmundson, 1965).…”

mentioning

confidence: 56%

Coordination complexes and catalytic properties of proteins and related substances. 83. Complete primary structure of the major component myoglobin of Pacific common dolphin (Delphinus delphis)

Wang¹,

Avila²,

Jones³

et al. 1977

Biochemistry

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The complete amino acid sequence of the major component myoglobin from Pacific common dolphin, Delphinus delphis, was determined by the automatic Edman degradation of several large peptides obtained by specific cleavages of the protein. More than 80% of the covalent structure was established by the degradation of the apomyoglobin and five peptides from: (1) cyanogen bromide cleavage at the two methionine residues, (2) trypsin cleavage of the acetimidated apomyoglobin at the three arginine residues, and (3) 2-p-nitrophenylsulfenyl-3-methyl-3'-bromoindolenine cleavage at the two tryptophan residues. The rest of the sequence was determined by use of the peptides prepared from further digestion of the central cyanogen bromide peptide with staphylococcal protease and trypsin. The primary structure of this myoglobin proved identical with that from the Atlantic bottlenosed dolphin, Tursiops truncatus, but showed four substitutions with respect to the sequence reported for the Black Sea dolphin which has also been given the designation Delphinus delphis.

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mentioning

confidence: 56%

Coordination complexes and catalytic properties of proteins and related substances. 83. Complete primary structure of the major component myoglobin of Pacific common dolphin (Delphinus delphis)

Wang¹,

Avila²,

Jones³

et al. 1977

Biochemistry

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“…The common residue found at position 54 is glutamic acid. Aspartic acid at this position has been found previously only in the myoglobins of the true seals (Bradshaw and Gurd, 1969;Nauman, 1973), the Black Sea dolphin (Kluh andBakardjieva, 1971), the chicken (Deconinck et al, 1975), and the sea hare (Tentori et ak, 1973).…”

Section: Discussionmentioning

confidence: 85%

“…This paper reports the application of the peptide fragmentation and analytical procedures that were used in these papers in determining the complete amino acid sequence of the myoglobin from the Atlantic bottlenosed dolphin, Tursiops truncatus. Completion of this sequence extends the number of complete Cetacean myoglobin sequences to 6, including the above mentioned Amazon River dolphin and California gray whale, the Black Sea dolphin (Kluh and Bakardjieva, 1971), common porpoise (Bradshaw and Gurd, 1969), and sperm whale (Edmundson, 1965).…”

mentioning

confidence: 85%

Complete amino acid sequence of the myoglobin from the Atlantic bottlenosed dolphin, Tursiops truncatus

Jones¹,

Vigna²,

Dwulet³

et al. 1976

Biochemistry

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The complete amino acid sequence of the major component myoglobin from the Atlantic bottlenosed dolphin, Tursiops truncatus, was determined by specific cleavage of the protein to obtain large peptides that are readily degraded by the automatic sequencer. Three easily separable peptides were obtained by cleaving the protein with cyanogen bromide at the 2 methionine residues and 4 peptides were obtained by cleaving the methyl acetimidated protein with trypsin at the 3 arginine residues. By subjecting 4 of these peptides and the apomyoglobin to automatic Edman degradation, over 80% of the covalent structure of the protein was obtained. The remainder of the primary structure was determined by further digestion of the central cyanogen bromide peptide with trypsin and staphylococcal protease. This myoglobin differs from that of the sperm whale, Physter catodon, at 15 positions, from that of the California gray whale, Eschrichtius gibbosus, at 14 positions, from that of the common porpoise, Phocoena phocoena, at 6 positions, and from the myoglobin of the Black Sea dolphin, Delphinus delphis and the Amazon River dolphin, Inia goeffrensis, at 5 and 7 positions, respecitvely. All substitutions observed in this sequence fit easily into the tertiary structure of sperm whale myoglobin.

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“…Bovine myoglobin (Han, Dautrevaux, Chaila, and Biserte, 1970); Harbor seal (Phoca Vitulina) and porpoise (Phocaena phocaena) myoglobins (Bradshaw and Gurd, 1969); Dolphin (Delphinus delphi@ myoglobin (Karadjova, Nedkov, Bakardjieva, and Genov, 1970;Kluh and Bakardjieva, 1971); Sperm whale (Physter catodon) myoglobin(Edmundson, t965); Echidna (Tachyglossus aculeatus) beta (Whittaker,Fisher,and Thompson,t972); Potorous tridactylus beta (Thompson and Air,197t), Kangaroo (Macropus giganteus) beta (Air and Thompson, 1969); Human gamma (Schroeder et al, 1963); Macaca mulatta beta (Matsuda, Maita, Ota, and Takei, 1970); Macaca [uscata beta (Matsuda et al, 1971); Langur (Presbytis entellus) beta (G. Matsuda, unpublished) ; Human beta (Braunitzer et al,t 961) ; Slow loris (Nycticebus coucang) beta (G. Matsuda, unpublished); Dog beta (Jones, Brimshall, and Duerst, 1971); Rabbit beta (Best,Flamm,and Braunitzer,t969); Horse beta (Smith and Chung, 1970;Dayhoff, t 972) ; Bovine fetal beta (Babin et al, 1966) ; Bovine beta B (Schroeder et al, 1967a;Dayhoff, 1972); Sheep beta B and C (Boyer et al, 1967;Dayhoff, 1972); to mammalian myoglobins. Thus in the first phylogeny not only must the separate genes coding for myoglobin and hemoglobin chains be attributed to a gene duplication which occurred when chordates and annelids still shared a common ancestor, but another gene duplication must also be postulated at this invertebrate stage of evolution for the origin of the lineage descending to lamprey globins.…”

Section: The Major Branches In;g Obin Phylogenymentioning

confidence: 99%

The phylogeny of human globin genes investigated by the maximum parsimony method

et al. 1974

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Abstract. Gene phylogenetic trees were constructed by the maximum parsimony method for various sets of ninety six globin chain amino acid sequences spanning plant and animal kingdoms. The method, executed by several computer programs, constructed ancestor and descendant globin messengers on tree topologies which required the least number of nucleotide replacements to account for the evolution of the globins. The human myoglobin-hemoglobin divergence was traced to a gene duplication which occurred either in the first vertebrates or earlier yet in the common ancestor of chordates and annelids, the alpha-beta divergence to a gene duplication in the common ancestor of teleosts and tetrapods, the gamma divergence from typical beta chains to a gene duplication in basal therian mammals, and the delta separation from beta to a duplication in the basal catarrhine primates. Evidence was provided by the globin phylogenies for the hominoid affinities of the gibbon and the close phyletic relationship of the African apes to man. Over the period of teleost-tetrapod divergence the globin messengers evolved at an average rate of t8.5 nucleotide replacements per t00 codons per 108 years, a faster rate than most previous estimates. Very fast and very slow rates were encountered in different globin lineages and at different stages of descent, reducing the effectiveness of globins as molecular clocks. Rates increased with gene duplication and decreased after selection discovered useful specializations in the products of genes which had previously been freer to accept mutations. The early eutherian radiation was characterized by rapid rates of globin evolution, but the later hominoid radiation by extremely slow rates. This pattern was related to more complicated grades of internal organization evolving in human ancestors. The types of nucleotide replacements in the globin messengers over the long course of globin evolution did not seem indicative of any special mutationalmechanisms.

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Primary structure of N‐terminal part of molecule of dolphin myoglobin

Cited by 30 publications

References 10 publications

Coordination complexes and catalytic properties of proteins and related substances. 83. Complete primary structure of the major component myoglobin of Pacific common dolphin (Delphinus delphis)

Coordination complexes and catalytic properties of proteins and related substances. 83. Complete primary structure of the major component myoglobin of Pacific common dolphin (Delphinus delphis)

Complete amino acid sequence of the myoglobin from the Atlantic bottlenosed dolphin, Tursiops truncatus

The phylogeny of human globin genes investigated by the maximum parsimony method

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