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Related Concept Videos

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,...
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...
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 14, 2026

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source
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Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

Published on: February 7, 2013

Standardization of Blood Haemoglobin Determinations

H B Collier

    Canadian Medical Association Journal
    |March 24, 2010
    PubMed
    Summary

    No abstract available in PubMed .

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