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  • 1
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. We have estimated the binding constant of 2,3-diphosphoglycerate (DPG) to llama and camel hemoglobin at 37°C and pH 6.7, 7.2, and 7.7 from the DPG induced change in the half saturation pressure (P 50). The values obtained were compared with the ones derived from similar measurements on human fetal and adult hemoglobin. At pH 7.2 the binding constant of DPG to llama deoxy-hemoglobin is smaller by a factor of 3 in comparison to camel hemoglobin whilst human fetal hemoglobin binds DPG six times less firmly than the human adult pigment. Camel and human adult hemoglobin have about the same affinity for DPG. 2. It is concluded that in llama hemoglobin an amino acid replacement at the DPG binding site explains the reduced phosphate affinity as compared to camel hemoglobin. In human fetal hemoglobin, in addition to an amino acid exchange, there are alterations of the anatomy of the DPG binding site which result in a poorer fit of the phosphate molecule. 3. Our data show that llama hemoglobin has a lower intrinsic oxygen affinity than camel hemoglobin so that despite the reduced DPG binding constant the oxygen affinity of llama and camel blood is very similar at equal phosphate concentration. Possibly, the amino acid exchange at the DPG binding site has compensated for the low oxygen affinity of llama hemoglobin in the course of phylogeny
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 303 (1983), S. 546-548 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The pygmy chimpanzee sequence is shown in Fig. 1, with supporting data in Fig. 2. There is no difference in this sequence from that of either chimpanzee or man, and only two differences from gorilla. At position a 23, gorilla has aspartic acid instead of glutamic acid and at £104, lysine ...
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  • 3
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Reactivation of genes due to physiological stress, such as induction of anaemia, is an important concept in the regulation of gene activity. The difference between the stress gene reported in chicken and the fetal genes of animals mentioned above is that the protein product of the stress gene could ...
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  • 4
    ISSN: 1432-1432
    Keywords: Monomeric hemoglobins ; Dimeric hemoglobins ; Chironomus ; Antibodies ; Evolution ; Gene duplication
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The monomeric hemoglobins ofChironomus tentans andC. pallidivittatus have been isolated and separated into their respective components by gel chromatography on Sephadex G-75 and ion-exchange chromatography on DEAE-Sephacel. The amino acid compositions of the purified components are given. The sequence of the 30 N-terminal amino acid residues of one of the monomeric components (Hb I fromC. pallidivittatus) was determined and found to be identical in almost all of its parts with the monomeric hemoglobins ofC. thummi (CTT III and CTT IV). Antibodies against the monomeric hemoglobins Hb I and Hb IIc and the dimeric fraction were highly specific and no cross reaction between dimeric and monomeric hemoglobins could be demonstrated. The antibodies against the monomers crossreact with the monomeric hemoglobins CTT III and CTT IV ofC. thummi. Taken together with genetic data, the immunological results indicate that divergence of monomeric from dimeric forms was an early event in the evolution of the various hemoglobins inChironomus.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 18 (1982), S. 102-108 
    ISSN: 1432-1432
    Keywords: Hemoglobin ; Myxine glutinosa ; Primary structure ; Heme linkage ; Phylogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Hagfish hemoglobin has three main components, one of which is Hb III. It is monomeric and consists of 148 amino acid residues (M = 17 350). Its complete primary structure, previously published, is discussed here. The proximal amino acid (F8) of the heme linkage is histidine as always in the hemoglobins, but the regularly expected distal histidine E7 is substituted by glutamine. This substitution, leading to a new kind of heme linkage, has hitherto only been demonstrated in opossum hemoglobin. It is suggested that E7, Gln, is directed out of the heme pocket, and that the adjacent Ell, Ile, is directed toward the inside of the pocket, giving the distal heme contact instead of histidine.Myxine Hb III has an additional tail of 9 amino acid residues at its N-terminal end, as has the hemoglobin ofLampetra fluviatilis. The genetic codes ofMyxine andLampetra hemoglobins show 117 differences, in spite of many morphological resemblances between hagfish and lamprey. Their primary hemoglobin structures show differences substantial enough to bo compatible with the divergence of the two families some 400–500 million years ago.
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  • 6
    ISSN: 1573-4943
    Keywords: Lynx ; carnivora ; hemoglobin ; primary structure ; homology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract 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, βA, βB, and α, 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 gasphase 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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  • 7
    ISSN: 1573-4943
    Keywords: Fur seal ; marine carnivora ; hemoglobin ; primary structure ; homology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The complete primary structure of the two hemoglobin components of the fur seal (Arctocephalus galapagoensis) is presented. The two components (HbI and HbII) occur in nearly equal amounts and have identical β-chains; whereas the two α-chains (αI/αII) differ by six exchanges Ile/Val, Met/Thr, Ser/Ala, Pro/His, Lys/Gly, and Thr/Ala at positions 10, 34, 35, 50, 78, and 131, respectively. The components were isolated by DEAE-Sephacel chromatography and were separated into the globin chains by RP-HPLC on a column of Nucleocil-C4. The sequences have been determined by Edman degradation in liquid- and gas-phase sequencer, using the native chains and tryptic peptides. The sequences compared with those of other Carnivora species and an adult human globin chains. An identical β-chain is found in fur seal and walrus, whereas larger differences were found between αI and αII compared to β-chains.
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  • 8
    ISSN: 1573-4943
    Keywords: Coati ; Carnivora ; hemoglobin ; primary structure ; phylogeney
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract 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 structure of globin chains and tryptic peptides was determined in liquid- and gas-phase sequenators. The sequence of the α and β-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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  • 9
    ISSN: 1573-4943
    Keywords: leopard ; hemoglobin ; primary structure ; physiology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The complete amino acid sequence of the major component of hemoglobin from amur-leopard (Panthera pardus orientalis) is presented. The major component accounts for more than 90% of the total hemoglobin. Separation of the globin subunits was achieved by ion-exchange chromatography on CM-cellulose in urea. The sequence was studied by automatic Edman degradation of tryptic and hydrolytic peptides. Alignment was carried out with human hemoglobin sequence. The β NH2 terminus is blocked with Ac-serine. The data are compared with other mammalian hemoglobins and results are discussed with respect to sequence and physiology.
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  • 10
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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