The Amino Acid Sequence of the Monomeric Hemoglobin Component from the Bloodworm, Glycera dibranchiata

Abstract

Abstract The complete amino acid sequence of 147 residues has been determined for the major monomeric component of the hemoglobin of the bloodworm, Glycera dibranchiata. The residues at 34 sites (23%) appear to be identical with those in sperm whale myoglobin. Of the 7 invariant residues found in vertebrate hemoglobins only three are present in this molecule: the glycine and phenylalanine residues at positions 27 (B6) and 45 (CD1), respectively, and the proximal heme-linked histidyl residue; the distal heme-linked histidine in vertebrate hemoglobins has been replaced by leucine.