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Related Concept Videos

Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

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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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Hemoglobin01:24

Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Related Experiment Video

Updated: Mar 24, 2026

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
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[Study on RBC Oxygen-Carrying Function with the Incubation Time].

Man Luo, Yuan-yuan Huang, Bao-chang Su

    Guang Pu Xue Yu Guang Pu Fen Xi = Guang Pu
    |March 12, 2016
    PubMed
    Summary

    Researchers studied red blood cells (RBCs) in vitro, observing how hemoglobin

    Area of Science:

    • Biophysics
    • Cell Biology
    • Spectroscopy

    Background:

    • Hemoglobin's oxygenation and deoxygenation cycle is crucial for red blood cell (RBC) structure and function in vivo.
    • Limited research exists on the oxygen-carrying function of individual living RBCs in vitro over time.

    Purpose of the Study:

    • To investigate changes in hemoglobin oxygen-carrying capacity and protein conformation in living RBCs cultured in vitro over a 24-hour period.
    • To correlate these molecular changes with the surface micromorphology of RBCs.

    Main Methods:

    • Confocal Raman scanning microscopy was used to collect Raman spectra from living erythrocytes.
    • Analysis focused on specific spectral peaks (1636, 1562 cm⁻¹) for hemoglobin oxygen carrying capacity and the amide III band (1240-1300 cm⁻¹) for protein conformation.

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  • Scanning electron microscopy (SEM) was employed to observe surface micromorphology.

    • Main Results:

    • Over 24 hours, hemoglobin exhibited alternating increases and decreases in oxygen uptake, with corresponding shifts between K (relaxed) and T (tense) states, indicating stable structure and allosteric function.
    • Red blood cell surface morphology, observed via SEM, showed alternating stretching and shrinking of the double concave disk shape.
    • These dynamic changes in oxygen carrying capacity and conformation were observed in individual living RBCs.

    Conclusions:

    • The study provides multi-level characteristic parameters from single living cells for in vitro RBC oxygen-carrying function research.
    • Findings offer potential research avenues for screening active components and evaluating drug efficacy and toxicity on RBCs in vitro.