[Hemoglobins of thecommon starling (Sturnus vulgaris, Passeriformes). The primary structures of the alphaA, alphaD and beta chains].

The primary structures of the major hemoglobin component HbA (alpha A- and beta-chains) and the minor component HbD (alpha D-chains, beta-chains are identical with those of HbA) of the Starling (Sturnus vulgaris) are given. The order Passeriformes, to which this species belongs, represents 5/8 of all species of birds. Comparing Starling and Greylag Goose (Anser anser) hemoglobins, HbA alpha A-chains differ by 20 amino acids or 23 nucleotides (3 two point mutations), beta-chains by 14 amino-acid and nucleotide exchanges. Eight substitutions modify alpha 1-beta 1 contacts and one phosphate contact (beta 2(NA2)His----Gln). In both chains some histidine residues are substituted by neutral amino acids. Comparing Starling and Pheasant (Phasianus colchicus colchicus) hemoglobins, HbD alpha D-chains differ by 33 amino acids or 39 nucleotides (6 two point mutations). Five alpha 1-beta 1 contacts, one alpha 1-beta 2-contact and one heme contact are changed. Valin was found in the N-terminal position of Starling alpha D-chains instead of methionin which is the N-terminus in all other avian alpha D-chains so far investigated. Not only alpha A- and beta-chains, but also alpha A- and alpha D-chains differ significantly from each other in the mutation rates. Substitutions are discussed in relation to evolution, function and physiology.