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1.
Carnivora: the primary structure of the hemoglobin from the silver fox (Vulpes vulpes var., Canidae)
The primary structure determination of the hemoglobin alpha- and beta-chains from the silver fox (Vulpes vulpes var., Canidae) is described. The separation of the chains could be achieved directly from the hemoglobin by RP-HPLC as well as by column chromatography of the globin using carboxymethyl-cellulose. Following tryptic digestion of the chains, the peptides were isolated by RP-HPLC. Amino-acid sequences were determined by Edman degradation in liquid and gas phase sequencers. The peptides could be aligned by homology with human and other Carnivora hemoglobins. Compared to human hemoglobin the alpha- and beta-chains of the silver fox exhibit 24 and 13 amino-acid exchanges, respectively. They differ by one alpha- and two beta-chain replacements from the domestic dog and the coyote. The substitutions affecting contact positions are discussed. 相似文献
2.
The hemoglobin of the Giant Otter (Pteronura brasiliensis, Carnivora) contains only one component. The complete primary structures of the alpha- and beta-chains are presented. 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 alpha-chains show 18 and the beta-chains 12 exchanges compared with human alpha- and beta-chains, respectively. In the alpha-chains, two substitutions involve alpha 1/beta 1-contacts and one a heme-contact. In the beta-chains one alpha 1/beta 1-, one alpha 1/beta 2- and one heme-contact are exchanged. The alpha- and beta-chains of the Giant Otter are compared to those of the Common Otter and other Carnivora hemoglobins. 相似文献
3.
H X Lin T Kleinschmidt G Braunitzer H G Scheil 《Biological chemistry Hoppe-Seyler》1988,369(5):349-355
The hemoglobin of the Common Otter (Lutra lutra, Carnivora) contains only one component. The complete primary structures of the alpha- and beta-chains are presented. They 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 alpha-chains show 18 and the beta-chains 13 substitutions compared to human alpha- and beta-chains, respectively. In the alpha-chains one heme- and two alpha 1/beta 1-contacts are exchanged. In the beta-chains the replacements involve one heme-, one alpha 1/beta 1-, and one alpha 1/beta 2-contact. The alpha- and beta-chains of the Common Otter are compared to those of other Carnivora hemoglobins. The unexpected low number of substitutions between Common Otter hemoglobin and that of Lesser Panda as well as of Harbor Seal is discussed. 相似文献
4.
The primary structure of the alpha- and beta-chains of hemoglobin from spotted hyena (Crocuta crocuta, Hyenidae) is presented. The structure-function relationship is discussed. The separation of the chains directly from hemoglobin was performed by RP-HPLC. After tryptic digestion of the chains, the peptides were isolated by RP-HPLC. Amino-acid sequences were determined by Edman degradation in liquid- and gas-phase sequencers. The alignment of the tryptic peptides was made by homology with human and other Carnivora hemoglobins. The hemoglobin from spotted hyena (Crocuta crocuta) exhibits in its alpha- and beta-chains 22 and 20 exchanges, respectively, compared to human hemoglobin. In the alpha-chains, two alpha 1 beta 1-contacts are exchanged. In the beta-chains five exchanges involve one alpha 1 beta 1-contact, one alpha 1 beta 2-contact, one heme contact, and two 2,3-DPG-binding sites. 相似文献
5.
The hemoglobin of the Indian false vampire Megaderma lyra 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, as well as of the prolyl-peptides obtained by acid hydrolysis of the Asp-Pro bond in the alpha- and beta-chains. The alpha-chains show 23 and the beta-chains 20 exchanges compared with the human alpha- and beta-chains, respectively. In the alpha-chains, three exchanges involved alpha 1/beta 1 contacts. In the beta-chains one heme-and three alpha 1/beta 1 contacts are exchanged. The functional and systematic aspects of these replacements are discussed. 相似文献
6.
The primary structure of the alpha- and beta-chains of hemoglobin from the Masked Palm Civet (Paguma larvata, Viverridae) is described. The chains were separated directly from hemoglobin by RP-HPLC. After tryptic digestion of the chains, the peptides were separated by RP-HPLC. Amino acid sequences were determined by Edman degradation in liquid and gas-phase sequencers. The alignment of the tryptic peptides was made by homology with human and other Carnivora hemoglobins. Paguma and human hemoglobin differ with respect to 23 amino-acid residues. Some of these amino-acid substitutions, which occur in both the alpha- and beta-chains, occur at contact sites between the subunits, and at the binding sites of heme and of organic phosphate, as well as involving residues responsible for the alkaline Bohr effect. 相似文献
7.
H X Lin T Kleinschmidt M L Johnson G Braunitzer 《Biological chemistry Hoppe-Seyler》1989,370(2):135-140
The primary structure of the alpha- and beta-chains of the hemoglobin from the Pacific Walrus (Odobenus rosmarus divergens, Pinnipedia) is presented. Sequence analysis revealed only one hemoglobin component whereas two bands were found in polyacrylamide gel electrophoresis. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid- and gas-phase sequencing of the chains and their tryptic peptides. The alpha-chains show 20 and the beta-chains 12 exchanges compared to the corresponding human chains. In the alpha-chains one heme- and two alpha 1/beta 1-contacts were exchanged whereas in the beta-chains one alpha 1/beta 1-, one alpha 1/beta 2-and one heme-contact are substituted. Compared to Harbour Seal (Phoca vitulina) the Walrus hemoglobin shows 9 amino-acid replacements in the alpha-chains and 5 in the beta-chains. The relation between Pinnipedia and Arctoidea is discussed. 相似文献
8.
The hemoglobin of the Brazilian Manatee (Trichechus inunguis, Sirenia) consists of one component. We present the primary structures of the alpha- and beta-chains which have been separated by chromatography on carboxymethyl-cellulose CM-52. The sequences have been determined by automatic Edman degradation with the film technique, using the native chains, tryptic peptides and the C-terminal prolyl-peptide obtained by acid hydrolysis of the Asp-Pro bond of the alpha-chains. Compared to the corresponding human chains we found 27 substitutions in the alpha- as well as in the beta-chains. Three heme contacts and four alpha 1/beta 1 contacts between the subunits are affected by exchanges. The hemoglobin of Trichechus inunguis is compared with those of Elephas maximus, Loxodonta africana, and Procavia habessinica and the monophyletic origin of the superorder Paenungulata is discussed. 相似文献
9.
S Stoeva T Kleinschmidt G Braunitzer H G Scheil 《Biological chemistry Hoppe-Seyler》1991,372(6):393-399
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 alpha- as well as the beta-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 alpha-chains and by 10 and 1 in the beta-chains, thus supporting the hyaenid character of the aardwolf. The exchanges at contact positions are shared by other carnivoran hemoglobins. 相似文献
10.
The erythrocytes of adult ratel contain two hemoglobin components, with two alpha- and one beta-chains. In this paper, their complete amino acid sequences are presented. The two alpha-chains differ in one residue at position 34 (Ala----Val) only. The primary structure of the chains was determined by sequencing the N-terminal regions (45 steps) and the tryptic peptides after their isolation from the digests by reversed-phase high-performance liquid chromatography. The alignment of these peptides was deduced from homology with other carnivora globins. The alpha-chains show 21 and the beta-chains 11 exchanges compared with human globin chains. In the alpha-chains, one heme- and two alpha 1/beta 1 contacts are exchanged. In the beta-chains there are three exchanges which involve one alpha 1/beta 1-, one alpha 1/beta 2- and one heme-contact. Between the ratel hemoglobin and those of carnivora a high degree of homology was found. 相似文献
11.
The hemoglobin of the Indian flying fox Cynopterus sphinx contains only one component. In this work, 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, as well as of the peptide obtained by acid hydrolysis of the Asp-Pro bond in the beta-chains. The alpha-chains show 14 and the beta-chains 19 exchanges compared with the human alpha- and beta-chains, respectively. In the alpha-chains one amino-acid exchange involves an alpha 1/beta 1 contact. In the beta-chains one heme contact, three alpha 1/beta 1- and one alpha 1/beta 2-contacts are exchanged. The functional and evolutionary aspects of these findings are discussed. 相似文献
12.
The complete primary structure of the hemoglobin from the bat Macrotus californicus (Chiroptera) is presented. This hemoglobin consists of only one component. The alpha- and beta-chains were separated by reverse phase high performance liquid chromatography. The sequences of both chains were established by automatic Edman degradation of the chains and the tryptic peptides, as well as of the C-terminal peptide obtained by acidic hydrolysis of the Asp-Pro bond in the beta-chains using the film- and gas-phase method. The sequences are compared with human hemoglobin: 15 amino-acid substitutions are found in the alpha- and 22 in the beta-chains. A comparison with the hemoglobin of Rousettus aegyptiacus and Myotis velifer shows a closer relation to the Mega- than to the Microchiroptera. 相似文献
13.
J G Sgouros T Kleinschmidt W Arnold G Braunitzer 《Biological chemistry Hoppe-Seyler》1986,367(3):223-228
The hemoglobin of the European marmot Marmota marmota marmota has been found to consist of only one component. In this work, we are presenting its primary structure. The globin chains have been separated by high performance liquid chromatography and the sequences have been determined by automated Edman degradation of the chains and their tryptic peptides, as well as of the peptide obtained by acid hydrolysis of the Asp-Pro bond in the beta-chains. In the alpha-chains we have found 13 and in the beta-chains 34 exchanges compared with the human alpha- and beta-chains, respectively. The amino acids which are substituted in the alpha-chains are not involved in any contacts, whereas in the beta-chains, one exchange involves a heme contact, two alpha 1/beta 1- and one alpha 1/beta 2-contacts. The functional and evolutionary aspects of these findings are discussed. 相似文献
14.
K Huber G Braunitzer D Schneeganss J K?sters F Grimm 《Biological chemistry Hoppe-Seyler》1988,369(6):513-519
The blood of the Rock-Hopper Penguin contains only one hemoglobin component, corresponding to the Hb A of other birds. The primary structures of the alpha- and beta-chains are presented. The chains were separated by high-performance liquid chromatography and cleaved either enzymatically (alpha) or both enzymatically and chemically (beta). Both the native chains and their peptides were sequenced using liquid and gas phase sequenators. The peptides were aligned using their homology to the sequence of human hemoglobin and other bird hemoglobins. As compared to human hemoglobin, 44 amino-acid replacements are found in the alpha-chains (68% homology) and 47 in the beta-chains (67.8% homology). These exchanges involve seven alpha 1/beta 1 and one alpha 1/beta 2 contact in the alpha-chains, whereas in the beta-chains eight alpha 1/beta 1, one alpha 1/beta 2 and one hem contact are substituted. The influence of these replacements on the structure-function relationships in hemoglobin, as well as their importance for the diving ability of penguins, are discussed. 相似文献
15.
T Kleinschmidt F A Bieber C F Nadler R S Hoffmann L N Vida G R Honig G Braunitzer 《Biological chemistry Hoppe-Seyler》1985,366(10):971-978
The hemoglobin of the ground squirrel Spermophilus townsendii consists of two components which are present in a ratio of ca. 2:1. The two hemoglobins have identical alpha-chains, but differ in their beta-chains. We present the primary structures of the alpha- and the two beta-globin chains. Following chain separation by chromatography on carboxymethyl-cellulose CM-52, the amino-acid sequences were established by automatic Edman degradation of the globin chains and the tryptic peptides, as well as of a peptide obtained by acid hydrolysis of the Asp-Pro bond of the beta-chains. The two beta-chains differ by only one amino-acid residue, Ala being present in the main and Asp in the minor component in position 58 (E2). The comparison with human hemoglobin showed only 14 exchanges in the alpha-chains but 33 in the beta-chains. Whereas no contact positions are affected in the alpha-chains, we found four such substitutions in the beta-chains, including one heme contact, two alpha 1/beta 1-contacts, and one alpha 1/beta 2-contact. It seems however, that the substitution found in the beta-chains has no effect on the oxygen affinity. 相似文献
16.
The adult Polar and Asiatic Black Bear have one hemoglobin component each. The complete amino-acid sequences of their alpha- and beta-chains are presented. Their primary structures were determined by sequencing the tryptic and prolyl peptides. The alignment of these peptides was deduced from homology to human hemoglobin chains. The hemoglobin sequences of the two species proved to be identical. The evolutionary aspects of this result are discussed. A table of identical hemoglobin sequences from different species is given. 相似文献
17.
The complete primary structure of the hemoglobin from the Pallid Bat (Antrozous pallidus, Microchiroptera) is presented. This hemoglobin consists of two components with identical amino-acid sequences, differing, however, in the N-terminus which is formylated in 12.5% of the beta-chains. The alpha- and beta-chains were separated by reversed phase high performance liquid chromatography. The sequences of both chains were established by automatic Edman degradation with the film technique or gas phase method using the native chains and the tryptic peptides. The formylation of a part of the N-terminal peptide of the beta-chains was determined by mass spectrometric examination. Compared to the corresponding human chains we found 14 substitutions in the alpha-chains and 21 in the beta-chains. One substitution in the alpha-chains and three in the beta-chains are involved in alpha 1/beta 1-contacts. Among these the exchange beta 123(H1)Thr----Cys is unusual because cysteine was so far not found in this position of mammalian beta-chains. Compared to the hemoglobin of Myotis velifer, another representative of the family Vespertilionidae, 5 residues are replaced in the alpha-chains and 18 in the beta-chains. 相似文献
18.
The coelacanth (Latimeria chalumnae, Actinistia) has a single hemoglobin component. The primary structures of the alpha- and beta-chains are presented. They could be separated by reversed-phase HPLC. Peptides obtained by tryptic digestion of the native and oxidized chains were isolated by reversed-phase HPLC and sequenced in liquid and gas-phase sequenators. The alignment was achieved by employing the N-terminal sequences of the native chains and those of a beta-chain cyanogen bromide peptide as well as fragments obtained by acid hydrolysis. The Latimeria alpha-chains consist of 142 amino-acid residues, due to a fish-specific insertion between positions 46 and 47, whereas the beta-chains are of normal length (146 residues). Latimeria alpha- and beta-chains share 72 (51.1%) and 70 (47.9%) identical residues with human hemoglobin, respectively. Numerous heme contacts and positions involved in subunit interface contacts are replaced. The most interesting of them were studied by molecular modeling. The loss of an alpha 1/beta 2-contact by the exchanges alpha 92(FG4)Arg----Leu and beta 43(CD2)Glu----Lys might be responsible for the easy dissociation of the tetrameric hemoglobin molecule. A comparison of the residues replaced in contact positions with fishes and amphibians revealed the highest number of matches between Latimeria and tadpoles. The same result was obtained by the evaluation of other regions relevant for structure and function of the molecule, like exon-intron boundary regions, phosphate binding sites and salt bridges responsible for the Bohr effect. 相似文献
19.
The primary structures of the alpha- and beta-chains of hemoglobin and myoglobin from the gundi (Ctenodactylus gundi, Rodentia) are presented. The sequences were determined after enzymatic and chemical cleavages of the polypeptide chains and by sequencing of the peptides mainly by automated sequence analysis. The sequences of gundi hemoglobin chains and of myoglobin are compared with those of other rodents. 相似文献
20.
G A Singer T Kleinschmidt J D Pettigrew G Braunitzer 《Biological chemistry Hoppe-Seyler》1991,372(12):1089-1095
The Australian ghost bat (Macroderma gigas, Microchiroptera) has two hemoglobin components in the ratio 3:2. They share identical beta-chains and differ by three replacements in the alpha-chains. The primary structures of all three chains are presented. They could be separated by high-performance liquid chromatography. The sequences were determined by automatic liquid and gas phase Edman degradation of the chains and their tryptic peptides. The two alpha-chains show 18 and 19 and the beta-chains 15 exchanges compared to human alpha- and beta-chains, respectively. The divergent evolution of Macroderma gigas and Megaderma lyra, two representatives of the family Megadermatidae, is discussed. An influence of replacements at functionally important positions on the hemoglobin oxygen affinity seems unlikely. 相似文献