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Structural and functional characterization of Delphinus delphis hemoglobin system.

Barbara Manconi1, Irene Messana, Federica Maggiani

  • 1Department of Applied Sciences to Biosystems, University of Cagliari, Cittadella Universitaria, 09042, Monserrato, CA, Italy.

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Dolphin hemoglobin (Hb) analysis reveals multiple beta and alpha globin types. These Hb variants show lower oxygen affinity and cooperativity compared to human HbA(0), with implications for diving adaptation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Marine Mammal Physiology

Background:

  • The hemoglobin (Hb) system is crucial for oxygen transport in vertebrates.
  • Understanding Hb structure and function in marine mammals like dolphins (Delphinus delphis) provides insights into adaptations for diving.
  • Previous studies suggest variations in cetacean Hb may relate to their unique physiological demands.

Purpose of the Study:

  • To characterize the structural and functional properties of the hemoglobin system in Delphinus delphis.
  • To investigate the molecular basis for differences in oxygen binding and cooperativity among dolphin Hb variants.
  • To compare dolphin Hb characteristics with human HbA(0) and other cetacean Hbs.

Main Methods:

  • High-Performance Liquid Chromatography (HPLC) coupled with Electrospray Ionization-Mass Spectrometry (ESI-MS) for globin analysis.
  • ESI-tandem mass spectrometry and nucleotide sequencing for identifying amino acid substitutions.
  • Anion-exchange chromatography for separating Hb fractions.
  • Oxygen binding assays to determine oxygen affinity, 2,3-bisphosphoglycerate (2,3-BPG) effect, and cooperativity.

Main Results:

  • Identified three major beta globins (beta1, beta2, beta3) and two major alpha globins (alpha1, alpha2) in Delphinus delphis.
  • Determined specific amino acid substitutions differentiating the beta and alpha globin variants.
  • Separated Hb into two fractions (HbI and HbII) with distinct globin compositions.
  • Both dolphin Hb fractions exhibited lower oxygen affinity, reduced 2,3-BPG sensitivity, and decreased cooperativity compared to human HbA(0), with HbII showing more pronounced differences.
  • Observed similarities between a dolphin Hb variant (HbII) and human HbJ-Cairo (Lysbeta65 --> Gln) in terms of decreased cooperativity.

Conclusions:

  • The Delphinus delphis hemoglobin system is characterized by high globin multiplicity and distinct functional properties.
  • Amino acid substitutions, particularly at position 5 of beta globins and position 65, likely influence oxygen binding, 2,3-BPG interaction, and cooperativity in cetacean Hbs.
  • The observed functional characteristics of dolphin Hb may represent adaptations for efficient oxygen management during prolonged diving.