Carnivora: Primary Structure of the Hemoglobins from Ratel<i>(Mellivora Capensis)</i>

Rodewald, Karin; Braunitzer, Gerhard; Göltenboth, R

doi:10.1515/bchm3.1988.369.2.1137

Cited by 7 publications

(5 citation statements)

References 11 publications

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“…370 (1978) parison with the Pacific walrus' 22^ and with the harbour seal' 23^ shows few differences with the corresponding chains of the ferret (Table 1). Most Carnivora species belong to Fissipedia.This second suborder of Carnivora was recently divided into two super-families, the Arctoidea and the Cynofeloidea [8] . The differences between the ferret chains and the corresponding sequences already described are given in Tables 2 and 3.…”

Section: Resultsmentioning

confidence: 99%

“…References in ref. [23) , except for the European polecat 1111 , the otters' 6 · 7 ', the ratel [8] and the spectacled bear [24] . change on the first base of the codon, the Met residue in the wild strain is replaced by Val in the ferret; a great variability may be noted at this position, as Gly, Leu, He are present in other Carnivora α-chains.…”

Section: Resultsmentioning

confidence: 99%

“…Whereas the covalent structure of the hemoglobins of two otters (Lutrinae) [6 -7] , as well as the sequence of the hemoglobin of the ratel (Mellivorinae) [8] are known, no data relative to the Mephitinae are available. In the Mustelinae, we have previously described the sequence of the -chain^ common to the two hemoglobins of the ferret (Mustela putorius furo), a polecat which has been domesticated at least since Roman times^.…”

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Carnivora: The Primary Structure of the α-Chains of Ferret (Mustela putorius furo,Mustelidae) Hemoglobins

Hombrados

Vidal²,

Rodewald³

et al. 1989

Biological Chemistry Hoppe-Seyler

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Ferret erythrocytes contain two hemoglobins differing only by their α-chains. The primary structure of the common j8-chain has been previously described; the complete sequence of the two α-chains are reported in this paper. The globin chains were separated by ion-exchange chromatography; the enchains (42 steps), their tryptic peptides as well as the prolyl-peptides were subjected to automatic liquidand gas-phase Edman degradation.The two α-chains are very similar, differing at only one position (Asp 15 -»Gly 15 ). Comparison with human hemoglobin α-chain shows 16 and 17 exchanges, for α τ and α π chains, respectively; two substitutions involve ot\l i contacts and one the heme contacts. A high degree of homology was noted when the α-chains were compared to the corresponding chains of other representatives of the Carnivora order. Carnivora: die Prim rstruktur der α-Ketten der Frettchen-H moglobinen (TVlustela putorius furo, Mustelidae)Zusammenfassung: Die Erythrozyten des Frettchens enthalten zwei H moglobine, die sich in ihren α-Ketten unterscheiden. Die Prim rstruktur der gemeinsamen /3-Kette wurde bereits beschrieben. In dieser Arbeit berichten wir ber die vollst ndige Aminos uresequenz der beiden α-Ketten. Nach Trennung der Globinketten durch Ionenaustauscher-Chromatographie, wurden die α-Ketten (42 Schritte), ihre tryptischen Peptide und das Prolyl-Peptid dem automatischen Fl ssigkeits-und Gasphasen-Edman-Abbau unterworfen. Beide α-Ketten unterscheiden sich nur in einer Aminos ure (Asp/Gly) in Pos. 15. Im Vergleich mit den Human-a-Ketten zeigen die FrettchenPolypeptide 16 Austausche in den a r und 17 in α π -Ketten. Eine H m-und zwei a 1 /3 1 -Bindungsstellen sind ver ndert. Die Frettchen-H moglobine und die der Carnivora erwiesen sich als weitgehend homolog.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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Carnivora: The Primary Structure of the α-Chains of Ferret (Mustela putorius furo,Mustelidae) Hemoglobins

Hombrados

Vidal²,

Rodewald³

et al. 1989

Biological Chemistry Hoppe-Seyler

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“…Alpha-and 13-hemoglobin sequences from ten species in six carnivore groups were used in this study: giant 12 17 16 22 21 17 18 11 14 15 21 18 18 17 9 12 19 16 20 11 6 15 12 18 15 11 8 20 15 5 21 14 23 17 21 panda (Ailuropoda melanoleuca) (Tagle et al 1986); lesser panda (Ailurus fulgens) (Tagle et al 1986); raccoon (Procyon lotor) (Brimhall et al 1978) in Procyonidae; bear (identical sequences from Ursus maritimus and U. thibetanus) and spectacled bear (Tremarctos ornatus) (Hofmann and Braunitzer 1987) in Ursidae; harbor seal (Phoca vitulina) (Watanabe et al 1986) in Phocidae; and badger (Meles meles) (Hombrados et al 1976;1978), ratel (Mellivora capensis) (Rodewald et al 1988), and common otter (Lutra lutra) (Lin et al 1988) in Mustelidae.…”

Section: Methodsmentioning

confidence: 99%

The giant panda is closer to a bear, judged by ?- and ?-hemoglobin sequences

et al. 1993

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Using a-and [3-hemoglobin sequences, we made a maximum likelihood inference as to the phylogenetic relationship among carnivores, including the two pandas, giant and lesser. Molecular phylogenetic studies up to 1985 had consistently indicated that the giant panda is more closely related to the bear than to the lesser panda. In 1986, however, a contradictory tree was constructed, using hemoglobins and so on, in which the two pandas link together (Tagle et al. 1986). In contrast to that tree, our conclusion supports the close relationship between bear and giant panda. The surface impression of a close relationship between the two pandas drawn from pairwise amino acid differences is explained by a rapid rate of hemoglobin evolution in the bear compared to that in the two pandas.

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“…Hämoglobine der Reptilien: Die Primärstrukturen der o/-und ß 1 In the broad collection of hemoglobin sequence data one of the biggest orders of tetrapods, the Squamata, is represented by only one complete sequence of the α-globin chains from the Viper [4] (a member of the suborder of Serpentes). In this paper we present the sequences of a-and -globin chains of the Common Iguana (Iguana iguana, a member of the suborder of Sauria).…”

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Hemoglobins of Reptiles. The Primary Structures of the α^I- and β^I-Chains of Common Iguana(Iguana iguana)Hemoglobin

Rücknagel

Braunitzer²,

Wiesner³

1988

Biological Chemistry Hoppe-Seyler

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The primary structures ofo: 1 -and 1 -chains from the hemoglobins of the Common Iguana (Iguana iguana) are presented. The globin chains were separated on CM-cellulose in 8M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the native chains, the tryptic peptides and a peptide obtained by cyanogen bromide cleavage. The sequences are compared with human hemoglobin. Amino-acid replacements at positions critical for structure and function of the hemoglobin are discussed. The requirements for binding of ATP and also of DPG as allosteric effectors at the ß-chains seem to be fullfilled. Comparison of the -chains with those of the Viper (Vipera aspis) shows 66 amino-acid substitutions. This number is in the same order of magnitude as the ones found by comparison with «-chains of crocodiles and mammals as well as with o^ -chains of a turtle and birds. This result points towards a period of independent evolution of the reptile lines leading to the Common Iguana on one hand and to the Viper on the other. This time span is comparable to the one separating mammals from reptiles. Hämoglobine der Reptilien: Die Primärstrukturen der o/-und ß 1 -Ketten des Hämoglobins des Grünen Leguans (Iguana iguana)Zusammenfassung: Die Primärstrukturen der a 1 -und ^-Ketten der Hämoglobine des Grünen Leguans (Iguana iguana) werden beschrieben. Die Globinketten wurden chromatographisch an CM-Cellulose in 8M Harnstoffpuffer getrennt. Die Aminosäure-Sequenzen wurden durch automatischen Edman-Abbau der nativen Ketten, der tryptischen Peptide und eines BromcyanPeptids ermittelt.Die Sequenzen werden mit Human-Hämoglobin verglichen. Aminosäure-Austausche an für Struktur und Funktion des Hämoglobins entscheidenden Positionen werden diskutiert.

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Carnivora: Primary Structure of the Hemoglobins from Ratel(Mellivora Capensis)

Cited by 7 publications

References 11 publications

Carnivora: The Primary Structure of the α-Chains of Ferret (Mustela putorius furo,Mustelidae) Hemoglobins

Carnivora: The Primary Structure of the α-Chains of Ferret (Mustela putorius furo,Mustelidae) Hemoglobins

The giant panda is closer to a bear, judged by ?- and ?-hemoglobin sequences

Hemoglobins of Reptiles. The Primary Structures of the α^I- and β^I-Chains of Common Iguana(Iguana iguana)Hemoglobin

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Carnivora: Primary Structure of the Hemoglobins from Ratel(Mellivora Capensis)

Cited by 7 publications

References 11 publications

Carnivora: The Primary Structure of the α-Chains of Ferret (Mustela putorius furo,Mustelidae) Hemoglobins

Carnivora: The Primary Structure of the α-Chains of Ferret (Mustela putorius furo,Mustelidae) Hemoglobins

The giant panda is closer to a bear, judged by ?- and ?-hemoglobin sequences

Hemoglobins of Reptiles. The Primary Structures of the αI- and βI-Chains of Common Iguana(Iguana iguana)Hemoglobin

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Hemoglobins of Reptiles. The Primary Structures of the α^I- and β^I-Chains of Common Iguana(Iguana iguana)Hemoglobin