Hemoglobin and subunit multiplicity in the rainbow trout (Oncorhynchus mykiss) hemoglobin system (original) (raw)

Abstract

Hemoglobin (Hb) multiplicity is a commonly used index of phylogenetic differentiation and molecular adaptation in fish. Despite improvements in technologies for characterizing protein structure, our knowledge of the component composition of the Hb system in rainbow trout, Oncorhychus mykiss, has remained almost unchanged through three decades. The Hb is considered to consist of four components, of which two (HbI and HbIV) have been extensively characterised with regard to structure and function. Using a variety of molecular techniques we demonstrate the presence of at least nine different Hb fractions composed of nine (five α and four β globin) chains, and that HbI and HbIV consist of two and five individual components, respectively. These findings indicate that the published data on trout HbI and HbIV refer to mixtures of isoHbs and need to be reappraised.

Key takeaways

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  1. Rainbow trout hemoglobin consists of at least nine distinct fractions and multiple globin chains.
  2. Previous studies mistakenly classified HbI and HbIV as homogeneous; they contain multiple components.
  3. Functional properties of HbI and HbIV differ significantly, affecting oxygen transport under varying conditions.
  4. Advanced techniques like ESI-MS and FPLC reveal higher hemoglobin multiplicity than previously understood.
  5. High hemoglobin multiplicity may enhance intracellular pH buffering and adapt to environmental variations.

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FAQs

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What is the significance of Hb multiplicity in rainbow trout hemoglobin system?add

The research reveals that rainbow trout exhibit at least nine distinct Hb components, enhancing oxygen transport adaptability to environmental variations.

How does HbI's oxygen binding compare to HbIV?add

HbI demonstrates a pH-independent oxygen affinity, while HbIV reveals a significant Bohr effect, adjusting to metabolic acidosis.

What methodologies were used to analyze the hemoglobin components?add

Ion-exchange FPLC, reverse phase-HPLC, and ESI-MS were employed to characterize and quantify different Hb components.

What explains the high globin chain diversity found in trout hemoglobin?add

The study identified five major α chains and four major β chains, facilitating complex functional roles in oxygen transport.

When were differences in hemoglobin components first noted among fish?add

Distinct Hb multiplicity in fish was recognized as early as the 1980s, but the specific complexities in Oncorhynchus mykiss are newly detailed.