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The complete amino acid sequence has been determined for hemoglobin V from the lamprey, Petromyzon marinus.This sequence differs at only 12 sites from the sequence proposed for the hemoglobin of another species of lamprey, Lampetra fhviatilis.The primary structure of Petromyzon hemoglobin is compared with those of other vertebrate hemoglobins and is discussed in terms of the results of x-ray diiYraction studies which indicate the presence of 2 residues not found in the sequence work.Suggestions concerning possible structure-function relationships are based in part on the hypothesis that residues which are identical or very similar in all hemoglobins may have the same functions.Lamprey Hemoglobin Vol.245, No. 22 Automatic Edman Degradation Toward the completion of the work a few sequences were confirmed and completed with the aid of a Beckman-Spinco Protein/Peptide Sequencer, model 890.The thiazolinone derivative of each amino acid was converted manually to the
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Li et al. (1970) studied this question.
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