Antarctic fish hemoglobin: an outline of the molecular structure and oxygen binding properties—I. Molecular structure

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Abstract

  • 1.

    1. The blood of 18 species of Antarctic teleosts of five families showed two hemoglobin components (Hb 1, 80–90%, and Hb 2, 5–15%) in Nototheniidae, a single hemoglobin in the harpagiferids, bathydraconid and rajid, and four components in a zoarcid species.

  • 2.

    2. The hemoglobins from 11 species were purified and, in six species, crystallized. Globin mixtures were prepared from each component.

  • 3.

    3. Pure globin chains were obtained from Hb 1 of five species and Hb 2 of two species. The two hemoglobins appeared to have a chain in common; their suggested structure is A2B2 (Hb 1) and B2C2 (Hb 2).

  • 4.

    4. The molecular weight and the amino acid composition of each pure globin chain has been determined. From these data and from preliminary results on the amino acid sequence, A appears to be an α-chain.

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