6 research outputs found

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

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

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    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

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

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    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

    Kristallisierte �-d-Glucopyranosidase des S��mandel-Emulsins

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    The primary structure of the hemoglobin from the grey-headed flying fox (pteropus poliocephalus) and the black flying fox (p.alecto, megachiroptera) Die primärstruktur der hämoglobine des graukopf-flughundes (pteropus poliocephalus) und des schwarzen flughundes (p. alecto, megachiroptera)

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    Die Primärstrukturen der Hämoglobine zweier Flughunde der Gattung Pteropus werden angegeben. Beide haben zwei Komponenten: Im Hämoglobin von P. alecto wurden zwei α-Ketten im Verhältnis 1:1 und zwei β-Ketten im Verhältnis 4:1 gefunden. Bei P. poliocephalus wurden eine α- und zwei α-Ketten nachgewiesen, die letzteren im Verhältnis 1:1. Nach der Trennung der GlobinKetten durch HochdruckFlüssigkeitschromatographie wurden die Sequenzen durch automatischen Edman-Abbau an den Ketten und den tryptischen Peptideń ermittelt. Verglichen mit Humanhämoglobin werden in den α-Ketten des Hämoglobins von P. alecto und P. poliocephalus 18 bzw. 19 Austausche gefunden, während in den β-Ketten beider Spezies 16/17 Substitutionen vorliegen. Diese Austausche betreffen bei P. alecto einen α1/β1 -Kontakt in den α-Ketten. In den β-Ketten beider Tiere sind zwei α1/β1-,ein α1/β2- und ein Häm-Kontakt gegenüber Humanhämoglobin substituiert. Die betroffenen Seitenketten sind in beiden Fällen die gleichen. Die funktionellen und systematischen Aspekte dieser Befunde werden diskutiert
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