Primary structure of two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.

@article{Suzuki1990PrimarySO,
  title={Primary structure of two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.},
  author={T. Suzuki and T. Takagi and T. Gotoh},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 21},
  pages={
          12168-77
        }
}
Two types of linker subunits (linkers 1 and 2) of the extracellular hemoglobin of Tylorrhynchus heterochaetus have been isolated as disulfide-linked homodimers by C18 reverse-phase chromatography. These subunits constituted 6 and 13%, respectively, of total protein area on the chromatogram. The complete amino acid sequences of linkers 1 and 2 were determined by automated Edman sequencing of the peptides derived by digestions with lysyl endopeptidase, trypsin, chymotrypsin, Staphylococcus aureus… Expand
Stoichiometry of Subunits and Heme Content of Hemoglobin from the Earthworm Lumbricus terrestris*
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