Hämoglobine, XVI. Die Aminosäuresequenz der α-Ketten der beiden Hauptkomponenten des Karpfenhämoglobins

Abstract

The constitution of the [alpha]-chain of both the main components from a carp hemoglobin is presented. The [alpha]-chain from each component gives identical amino acid analyses. For the determination of the sequence, tryptic and peptic peptides of the complete chain were used and their separation was accomplished by column chromatography. The tryptic peptides form the basis for the elucidationof the primary structure. A comparison of the amino acid sequence with homologous chains from human hemoglobin shows an essentially higher exchange rate of amino acids than that with the [alpha]-chains of hemoglobins from higher animals. 67 amino acid exchanges were found. In contrast to mammalian [alpha]-chains, it can be observed that in addition there are 2 insertions and one deletion, each of one amino acid. Two of these mutations occur in a helical region, and it is thought that the tertiary structure of the carp [alpha]-chain is different.