The Amino Acid Sequence of the Adult Sumatran Tiger (Panthera tigris, Carnivora) Hemoglobins

The complete amino-acid sequences of the hemoglobins from the adult Sumatran tiger (Panthera tigris sumatrae) have been determined on automatic liquid- and gas-phase sequenators. The globin chains were isolated by reverse phase HPLC on a column of Nucleosil-C4.7V-Acetylserine was detected by FAB-mass spectroscopy as TV-terminal amino acid residue of the βI chain. Comparing the sequences of the globin chains of the tiger with that of human Hb-A, 23 substitutions were recognized in the a, 29 in βI and 28 in the βII chain

The complete primary structure of the marine carnivora, galapagoes fur seal (Arctocephalus galapagoensis, Otariidae) hemoglobins

Jahan M, Ahmed A, Trillmich F, Braunitzer G. The complete primary structure of the marine carnivora, galapagoes fur seal (Arctocephalus galapagoensis, Otariidae) hemoglobins. Journal of Protein Chemistry. 1991;10(3):257-263

Hemoglobin E B-Thalassemia in a Pakistani Family

Hemoglobin E is a slow moving B chain variant of hemoglobin, first discovered by Itano1. Characterized by Hunt et al2 showed glutamic acid at B 26 to be replaced by lysine. It is a common variant of hemoglobin in the world and reported in high frequency from South-East Asia3-6. Cases of Hb E, in combination with thalassemia have been reported on the basis of electrophoretic pattern only. In this communication a case of Hb E with B thalassemia is reported on the basis of amino acid sequencing of the abnormal peptide

Die Primärstruktur des Hämoglobins des Flu;-Manatis (Trichechus inunguis, Sirenia

The hemoglobin of the Brazilian Manatee {Trichechus inunguis, Sirenia) consists of one component. We present the primary structures of the α- and β-chains which have been separated by chromatography on carboxy-methyl-cellulose Cm-Kresol52. 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 α-chains.Compared to the corresponding human chains we found 27 substitutions in the α- as well as in the ß-chains. Three heme contacts and four α1 /β1 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. © 1988, Walter de Gruyter. All rights reserved

The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega.

The complete primary structure of the proteinase omega isolated from the latex of the Carica papaya fruits is given. The polypeptide chain contains 216 amino-acid residues, the alignment of which was deduced from sequence analyses of the native enzyme, the tryptic, chymotryptic, peptic and thermolysinolytic peptides and facilitated due to the considerable degree of homology with papain and actinidin. The location of the three disulfide bridges could be established with the help of peptic and thermolysinolytic fragments. Proteinase omega shares 148 identical amino-acid residues (68.5%) with papain and 108 ones (50%) with actinidin, including the three disulfide bridges and the free cysteine residue required for activity, as well as most of the other amino-acid residues involved in the catalytic mechanism and two thirds of the glycine residues which are of structural significance. The homology with other cysteine proteinases of different origin is discussed.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Direkte Reziproke Allosterische Wechsehvirkung von Sauerstoff und Hydrogencarbonat: Die Sequenz Der Hämoglobine von Kaiman (Caiman Crocodylus), Nil-Krokodil (Crocodylus Niloticus) und Mississippi-Krokodil (Alligator Mississippiensis)

Zur Untersuchung der Struktur-Funktionsbeziehungen wurden drei Hämoglobine der Crocodilia, des Kaimans, des Nil-Krokodils und des Mississippi-Krokodils komplett sequenziert: alle Hämoglobine zeigen in der Elektrophorese eine einzige Bande. Die Peptidkctten wurden automatisch und komplett mit dem Quadrolund - für Peptide - mit dem Propin-programm nach der Filmtechnik sequenziert. Die komplette Sequenz (841 Aminosäuren) wird gegeben und die Daten werden mit der Primärstruktur des menschlichen Hämoglobins verglichen. Die Zahl der Aminosäurcaustausche der β-Ketten ist außerordentlich groß und beträgt 74 bzw. 75 Reste und ist größer als die Unterschiede, die beim Vergleich der Hämoglobine der Säuger mit Fischen (64) und Vögeln (42) gefunden warden. Diese Daten bestätigen, daß die Zahl der akzeptierten Mutationen der Hämoglobine während der Evolution entschieden durch “Wechsehvirkung beeinflußt wird.Insbesondere wird die Frage der Kontrolle der O2-Affi-nität dieser Hämoglobine durch Hydrogencarbonat diskutiert, das als heterotroper allosterischer Effektor (ohne ATP, GTP, Inosinpentaphosphat oder 2,3-Diphosphoglycerat) in direkter Wechsehvirkung mit dem Sauerstoff steht. Aus den Sequenzdaten der Crocodilia und dem Rontgenmodell können die Bindungsstellen des Hydrogencarbonats alsβ1, β82 und β144 ermittelt werden, wobei β144 Glutaminsäure, die bei alien Crocodilia vorliegt, von besonderer Bedeutung für die Bildung einer Wasserstoffbrücke vom Hydrogencarbonat zu einem der Sauerstoffe des Glutamats ist. © Copyright by Walter de Gruyter & CoSCOPUS: ar.jinfo:eu-repo/semantics/publishe

The Primary Structure of the Hemoglobin from the Tomb Bat (Taphozous georgianus, Microchiroptera)

The primary structures of the α- and β-chains of the single hemoglobin component from the tomb bat (Taphozous georgianus, Microchiroptera) are presented. After chain separation by reversed-phase HPLC the sequences could be determined by automatic gas and liquid phase Edman degradation of the chains and their tryptic peptides. The α- and β-chains differ from human hemoglobin by 14 and 18 replacements, respectively. Compared to the total number of amino-acid exchanges, the exchange rate in the interhelical regions of the α-chains is surprisingly high (25%). It seems unlikely that substitutions at contact positions affect the oxygen binding properties of the hemoglobin