Das Hämoglobin des adulten Andenkondors(Vultur gryphus, Cathartiformes)
- 1 January 1985
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 366 (2) , 1141-1148
- https://doi.org/10.1515/bchm3.1985.366.2.1141
Abstract
The complete amino-acid sequence of the .alpha.A- and the .beta.-chains of the major component (HbA) and the .alpha.D- and the .beta.-chains of the minor component (HbD) of Andean Condor (Vultur gryphus) is presented. The minor component with the .alpha.D-chains is present in smaller amounts (17%) than in other birds (25%). The comparison with the corresponding chains of Greylag Goose (Anser anser) shows 17 different amino acids (17 nucleotides, only one-point mutations) in the .alpha.A-chains and 8 (8 nucleotides) in the .beta.-chains. The .alpha.D-chains differ from those of the pheasant (Phasianus colchicus colchicus) in 24 amino acids (27 nucl., 3 two-point mutations). Seven .alpha.1.beta.1-, one .alpha.1.beta.2- three .alpha.1.alpha.1-contacts and one .beta.1.beta.1-contact are exchanged. The systematics of Cathartiformes, Ciconiiformes and Phoenicopteriformes is discussed, based on the amino-acid exchanges of all known adult hemoglobins of birds.This publication has 16 references indexed in Scilit:
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