Cardiopulmonary Anatomy & Physiology
Cardiopulmonary Anatomy & Physiology
7th Edition
ISBN: 9781337794909
Author: Des Jardins, Terry.
Publisher: Cengage Learning,
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Chapter 6, Problem 2RQ
Summary Introduction

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With no oxygen, hemoglobin (Hb) is found in a tense state, that is, it has less affinity for oxygen. When the oxygen level increases, the binding affinity for hemoglobin also increases. When % (percent) hemoglobin saturation of the y-axis is plotted against the partial pressure of oxygen (mm Hg or millimeter of mercury) on the x-axis, we get an S-shaped curve. This indicates that with an increase in oxygen, more hemoglobin binds to it, which is known as the relaxed state. This phenomenon of oxygen binding readily at the relaxed state of hemoglobin is known as cooperativity. When hemoglobin is 100% saturated with oxygen, the S-shaped curve levels out eventually.

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