Carnivora: The Primary Structures of Adult Lion (Panthern leo) Hemoglobins

Jahan, Meeno; Ahmed, Aftab; Braunitzer, Gerhard; Zaidi, Zafar H.; Göltenboth, R

doi:10.1515/znb-1987-1116

Cited by 3 publications

(1 citation statement)

References 10 publications

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“…Most of these residues are typical for Carnivora rather than supporting the assumption that Hyaenidae are specialized Viverridae [5i6 ' 9] . Besides Hyaenidae and Viverridae, the superfamily Aeluroidae includes Herpestidae and Felidae [ Brought to you by | Purdue University Libraries Authenticated Download Date | 6/12/15 5:39 AM tran tiger (Panthera tigris sumatrae)^2 2 \ jaguar (Panthera oncaf 2^, Amur leopard (Panthera pardus orientalis) [24] and lion (Panthera leo) [25] . Whereas the achains of Proteles, Crocuta and Paguma only share o:4Ser as a typical amino-acid residue with the four Panthera species, several such residues can be found in the ß-chains.…”

Section: Resultsmentioning

confidence: 99%

The Primary Structure of the Hemoglobin from the Aardwolf(Proteles cristatus,Hyaenidae)

Stoeva

Kleinschmidt²,

Braunitzer³

et al. 1991

Biological Chemistry Hoppe-Seyler

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The hemoglobin of the aardwolf (Proteles cristatus) contains only one component. In this paper, we are presenting its primary structure. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas-phase Edman degradation of the chains and their tryptic peptides.The a-as well as the /3-chains show 20 exchanges compared with the corresponding human chains. The difference to the masked palm civet (Paguma larvata) and the spotted hyaena (Crocuta crocuta) is marked by 16 and 4 replacements in the -chains and by 10 and 1 in the /3-chains, thus supporting the hyaenid character of the aardwolf. The exchanges at contact positions are shared by other carnivoran hemoglobins.Zusammenfassung: Die Erythrocyten des Erdwolfs (Proteles cristatus) enthalten nur eine Hämoglobin-komponente. Ihre Primärstruktur wird angegeben. Nach Trennung der Globinketten durch HochdruckFlüssigkeitschromatographie wurden die Sequenzen durch automatischen Edman-Abbau an den Ketten und den tryptischen Peptiden bestimmt. Verglichen mit Humanhämoglobin werden in beiden Ketten je 20 Austausche gefunden. Vom Larvenroller (Paguma larvata) und derTüpfelhyäne (Crocuta crocuta) unterscheidet sich das Prote/es-Hämoglobin durch 16 bzw. 4 Substitutionen in den -Ketten und durch 10 bzw. l in den /3-Ketten, wodurch der Erdwolf als zu den Hyä-nen gehörig charakterisiert wird. Die in Bindungsstellen zum Häm und zwischen den Untereinheiten gefundenen Substitutionen sind auch bei anderen Carnivora-Hämoglobinen vorhanden.

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Section: Resultsmentioning

confidence: 99%

The Primary Structure of the Hemoglobin from the Aardwolf(Proteles cristatus,Hyaenidae)

Stoeva

Kleinschmidt²,

Braunitzer³

et al. 1991

Biological Chemistry Hoppe-Seyler

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Carnivora: The primary structure of hemoglobin from adult coati(Nasua nasua rufa, Procyonidae)

1990

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The complete primary structure of the hemoglobin from the adult coati (Nasua nasua rufa) is presented. The erythrocytes contain one hemoglobin component and two globin chains. The isolation of globin chains was achieved by reversed-phase HPLC on a column of Nucleosil-C4. The primary structures of globin chains and tryptic peptides was determined in liquid- and gas-phase sequenators. The sequence of the alpha and beta-chains of coati compared with those of other Carnivora species. Results are discussed with respect to structural variations and the phylogenetic relationship.

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Carnivora: The primary structure of the major hemoglobin component from adult European lynx (Lynx lynx, Felidae)

1992

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The complete primary structure of the major hemoglobin component from the adult European lynx (Lynx lynx) is presented. Presence of two hemoglobin components and three chains, beta A, beta B, and alpha, identified by gel electrophoresis. The purification of the globin chains achieved by ion-exchange chromatography. The globin chains were digested with trypsin. The peptide generated were purified by reversed-phase HPLC. Sequencing of the native chains up to 42 cycles and of the tryptic peptides were deduced by Edman degradation in liquid- and gas-phase sequencer. The primary structure established aligned with those of human Hb-A. The comparison of lynx globin chains with other representatives of the Felidae, lion, tiger, jaguar, leopard, and cat revealed high homology.

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Carnivora: The Primary Structures of Adult Lion (Panthern leo) Hemoglobins

Cited by 3 publications

References 10 publications

The Primary Structure of the Hemoglobin from the Aardwolf(Proteles cristatus,Hyaenidae)

The Primary Structure of the Hemoglobin from the Aardwolf(Proteles cristatus,Hyaenidae)

Carnivora: The primary structure of hemoglobin from adult coati(Nasua nasua rufa, Procyonidae)

Carnivora: The primary structure of the major hemoglobin component from adult European lynx (Lynx lynx, Felidae)

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