Hämoglobine, XLVI. Die Primärstruktur der α-Ketten des Hämoglobins vom Gürteltier (Dasypus novemcinctus,Edentata)
- 1 January 1982
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 363 (1) , 239-246
- https://doi.org/10.1515/bchm2.1982.363.1.239
Abstract
The complete primary structure of the identical .alpha.-chains of the 2 Hb components of armadillo (D. novemcinctus) is presented. It was established on the tryptic peptides by automatic Edman degradation. The alignment was done according to the homology with human .alpha.-chains. Twenty-five differences were found beteen both chains. A comparison of the functional amino acid residues shows 1 substitution in the surrounding of the heme, 3 in the .alpha.1.beta.1- and 2 in the .alpha.1.beta.2-subunit interface. The 2 replacements .alpha.38(C3)Thr .fwdarw. Pro and .alpha.44(CD2)-Pro .fwdarw. Ser may contribute to high O2 affinity of the armadillo Hb by destabilization of the T-structure.This publication has 12 references indexed in Scilit:
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