Hemoglobin of the Adult White Stork(Ciconia ciconia,Ciconiiformes). The Primary Structure of αA- and β-Chains from the Only Present Hemoglobin Component

Abstract

The hemolysate obtained from erythrocytes of the adult White Stork (Ciconia ciconia) contains only 1 Hb component, identified as HbA. The complete primary structures of .alpha.A- and .beta.-chains are presented. The minor Hb component HbD with .alpha.D-chains usually present in adult avian species was not detected in the White Stork. The sequence was determined by automatic Edman degradation of tryptic peptides and in the case of .beta.-chains the C-terminal peptide was obtained by chemical cleavage at the Asp-Pro bond. Homologous comparison with the greylag goose (Anser anser) Hb showed that the .alpha.A-chains differ by 23 amino-acid exchanges, the .beta.-chains by 17. Of the substitutions in the .alpha.A-chains 4 are in the .alpha.1.beta.1-contact points, 1 in the .alpha.1.beta.2-contacts and 1 in the amino acids near the heme. The amino-acid substitutions of the white stork Hb are compared to the other avian Hb. .alpha.D-chain is probably a persistence of an embryonic gene.