PRIMARY STRUCTURE OF THE HEMOGLOBIN OF THE GREYLAG GOOSE AND THE UNEQUAL EVOLUTION OF THE BETA-CHAINS (AN EXPERIMENTAL APPROACH TO A BIOCHEMICAL-ANALYSIS OF BEHAVIOR)

Abstract

The primary structures of the .alpha.- and .beta.-chains from greylag goose (A. anser) Hb 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, the mutation rate of the .alpha.-chains was normal, i.e., 6 million years/mutation. This corresponds to the values for other species. The mutation rate of .beta.-chains was reduced and calculated at 25 million years/mutation. This is possibly due to a specific function of .beta.-chains. The ability of bar-headed goose (A. indicus) to fly and breathe at high altitudes was explained on a molecular basis.