Amino acid sequence of polypeptide chain IIB of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.

@article{Suzuki1985AminoAS,
  title={Amino acid sequence of polypeptide chain IIB of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.},
  author={T. Suzuki and H. Yasunaga and T. Furukohri and K. Nakamura and T. Gotoh},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 21},
  pages={
          11481-7
        }
}
The giant extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus consists of two types of subunits: a "monomeric" chain (chain I) and a disulfide-bonded trimer of chains IIA, IIB, and IIC. The complete amino acid sequence of chain IIB was determined. This chain has 148 amino acid residues and a molecular weight of 17,236 including a heme group. Of the residues in chain IIB, 74 (50%) and 34 (30%) were found to be identical with those in the corresponding positions in… Expand
Subunit assembly of giant haemoglobin from the polychaete Tylorrhynchus heterochaetus.
Adventitious variability? The amino acid sequences of nonvertebrate globins.
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References

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Amino Acid Sequence of Tylorrhynchus Hemoglobin
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