| Abstract: | The primary structures of the alpha- and beta-chains from greylag goose (Anser anser) hemoglobin are given. The sequence was deduced automatically in the sequenator. They differ from chicken alpha-chains in the exchange of 30, from beta-chains in the exchange of only 8 amino acid residues, respectively. The contact points of inositol pentaphosphate with the beta-chains are identical in chicken and greylag goose. Unequal evolution of the beta-chains was found, which is published here for the first time. By comparing the sequences of chicken and greylag goose and considering paleontological data, we found the mutation rate of the alpha-chains to be normal, i.e. 6 million years/mutation. This corresponds to the values for other species. The mutation rate of beta-chains is reduced and was calculated at 25 million years/mutation. This is possibly due to a specific function of beta-chains. This paper is the basis of our attempt to explain on a molecular basis the ability of bar-headed goose (Anser indicus) to fly and breathe at high altitudes. |
