[Hemoglobins. XXVII. The amino acid sequence of hemoglobin III from Myxine glutinosa L. A new hemecomplex: E7 glutamine, E11 isoleucine].

The sequence analysis of the main component, "HbIII", of the hemoglobins from the hagfish (Myxine glutinosa L.) is described. The hagfish belongs to the Cyclostomata, the most primitive class of the vertebrates. The hagfish hemoglobin displays a great heterogeneity, as described earlier. It consists of several monomeric hemoglobins. The globin of HbIII was isolated and used for the sequence analysis. The tryptic peptides as well as the cyanogen bromide and the BNPS-skatol fragments were separated. The sequences of the peptides were determined automatically by the help of a sequenator. Compared with other hitherto analyzed vertebral hemoglobins, also including other Cyclostomata, the primary structure of "HbIII" differs by more than 50%. The differences are so many that one can refer the Myxine hemoglobin neither as an alpha- nor as a beta-chain (of the tetrameric hemoglobins). The hagfish hemoglobin like other Cyclostomata has an additional segment of 9 residues at the amino terminus end compared with the mammalian hemoglobins. In the F-helix there is an insertion of 3 amino acid residues and in the interhelical gap, GH, there is a deletion of 9 residues. The substitutions of the residues forming the heme complex are of special interest. The distal histidine, E7, is substituted for glutamine. The proximal histidine, F8, is invariable. The valine E11 is substituted by isoleucine and the leucine FG3 by phenylalanine. These positions are involved in the contact with the heme group. This complex has never been described before.