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Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
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When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
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Red algae, also known as rhodophytes, are primarily found in marine environments, though some species inhabit freshwater and terrestrial ecosystems. These organisms exist in both unicellular and multicellular forms, with some multicellular varieties reaching macroscopic sizes.As phototrophic organisms, red algae contain chlorophyll a; however, their chloroplasts lack chlorophyll b. Instead, they possess phycobiliproteins, which serve as major light-harvesting pigments, similar to those found in...
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Respiratory Responses of the Blue Crab Callinectes sapidus to Long-Term Hypoxia.

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BIVALVE HEMOCYANIN: STRUCTURAL, FUNCTIONAL, AND PHYLOGENETIC RELATIONSHIPS.

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Updated: Feb 16, 2026

Measuring Deformability and Red Cell Heterogeneity in Blood by Ektacytometry
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Red Blood Cell Oxygen Binding in Capitellid Polychaetes.

C P Mangum, J M Colacino, J P Grassle

    The Biological Bulletin
    |January 7, 2018
    PubMed
    Summary

    Red blood cell oxygen equilibrium properties are species-specific in capitellid polychaetes, showing greater variation than related species. These differences may reflect adaptations to environmental temperature or body size.

    Area of Science:

    • Marine Biology
    • Comparative Physiology
    • Biochemistry

    Background:

    • Red blood cells (RBCs) facilitate oxygen transport in many animals.
    • Oxygen equilibrium properties, including affinity and cooperativity, are crucial for efficient gas exchange.
    • Capitellid polychaetes, marine annelids, possess coelomic RBCs with largely uncharacterized oxygen-binding capabilities.

    Purpose of the Study:

    • To investigate and compare the oxygen equilibrium properties of RBCs across 10 morphologically similar capitellid polychaete species.
    • To determine if these properties are species-specific and to assess the range of variation.
    • To explore potential ecological or physiological drivers for observed differences.

    Main Methods:

    • Collection and preparation of red blood cells from 10 capitellid polychaete species.

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  • Measurement of oxygen equilibrium curves to determine oxygen affinity (P50) and cooperativity (Hill coefficient).
  • Comparative analysis of oxygen-binding parameters among species.

    • Main Results:

    • Oxygen equilibrium properties of RBCs were found to be generally species-specific among the studied capitellid polychaetes.
    • Significant differences in oxygen affinity were observed between most species.
    • Cooperativity of oxygen binding also varied notably in several species, exceeding the range seen in related polychaetes.

    Conclusions:

    • The observed species-specific variations in RBC oxygen affinity and cooperativity suggest significant adaptive divergence within capitellid polychaetes.
    • These differences may be adaptations to varying environmental thermal properties or differences in body size.
    • Further research is warranted to elucidate the precise selective pressures driving these distinct oxygen-binding characteristics.