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Related Concept Videos

Hemoglobin01:24

Hemoglobin

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...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

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,...
Blood Studies I: ABG and VBG01:26

Blood Studies I: ABG and VBG

Blood studies are critical in the medical field, enabling healthcare professionals to assess a patient's health status accurately. This page will focus on two significant blood studies: Arterial Blood Gas (ABG) and Venous Blood Gas (VBG).
Arterial Blood Gas (ABG)
Arterial Blood Gas (ABG) studies are crucial for assessing the lungs' ability to supply oxygen and remove carbon dioxide, reflecting the patient's ventilation status. They also help understand the kidneys' capacity to reabsorb or...

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Related Experiment Video

Updated: Jun 9, 2026

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering
05:18

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

Published on: December 7, 2016

Haemoglobinometry

C Rimington

    British Medical Journal
    |August 27, 2010
    PubMed
    Summary

    No abstract available in PubMed .

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