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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and the proximal heme-linked histidyl residue; the distal heme-linked histidine in vertebrate hemoglobins has been replaced by leucine.
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Imamura et al. (1972) studied this question.
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