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Shape of red blood cells

This photograph shows a few red blood cells.
Erythrocytes are biconcave discs with very shallow centers. This shape optimizes the ratio of surface area to volume, facilitating gas exchange. It also enables them to fold up as they move through narrow blood vessels.


Hemoglobin is a large molecule made up of proteins and iron. It consists of four folded chains of a protein called globin    , designated alpha 1 and 2, and beta 1 and 2 ( [link] a ). Each of these globin molecules is bound to a red pigment molecule called heme    , which contains an ion of iron (Fe 2+ ) ( [link] b ).


This figure shows the structure of hemoglobin. The left panel shows the protein structure and the right panel shows the chemical formula.
(a) A molecule of hemoglobin contains four globin proteins, each of which is bound to one molecule of the iron-containing pigment heme. (b) A single erythrocyte can contain 300 million hemoglobin molecules, and thus more than 1 billion oxygen molecules.

Each iron ion in the heme can bind to one oxygen molecule; therefore, each hemoglobin molecule can transport four oxygen molecules. An individual erythrocyte may contain about 300 million hemoglobin molecules, and therefore can bind to and transport up to 1.2 billion oxygen molecules (see [link] b ).

In the lungs, hemoglobin picks up oxygen, which binds to the iron ions, forming oxyhemoglobin    . The bright red, oxygenated hemoglobin travels to the body tissues, where it releases some of the oxygen molecules, becoming darker red deoxyhemoglobin    . Oxygen release depends on the need for oxygen in the surrounding tissues, so hemoglobin rarely if ever leaves all of its oxygen behind. In the capillaries, carbon dioxide enters the bloodstream. About 76 percent dissolves in the plasma, some of it remaining as dissolved CO 2 , and the remainder forming bicarbonate ion. About 23–24 percent of it binds to the amino acids in hemoglobin, forming a molecule known as carbaminohemoglobin    . From the capillaries, the hemoglobin carries carbon dioxide back to the lungs, where it releases it for exchange of oxygen.

In patients with insufficient hemoglobin, the tissues may not receive sufficient oxygen, resulting in another form of anemia. In determining oxygenation of tissues, the value of greatest interest in healthcare is the percent saturation; that is, the percentage of hemoglobin sites occupied by oxygen in a patient’s blood. Clinically this value is commonly referred to simply as “percent sat.”

Percent saturation is normally monitored using a device known as a pulse oximeter, which is applied to a thin part of the body, typically the tip of the patient’s finger. The device works by sending two different wavelengths of light (one red, the other infrared) through the finger and measuring the light with a photodetector as it exits. Hemoglobin absorbs light differentially depending upon its saturation with oxygen. The machine calibrates the amount of light received by the photodetector against the amount absorbed by the partially oxygenated hemoglobin and presents the data as percent saturation. Normal pulse oximeter readings range from 95–100 percent. Lower percentages reflect hypoxemia    , or low blood oxygen. The term hypoxia is more generic and simply refers to low oxygen levels. Oxygen levels are also directly monitored from free oxygen in the plasma typically following an arterial stick. When this method is applied, the amount of oxygen present is expressed in terms of partial pressure of oxygen or simply pO 2 and is typically recorded in units of millimeters of mercury, mm Hg.

Questions & Answers

Definition of respiration
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in the mouth
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stimulates the follicle to release the mature ovum into the oviduct
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Source:  OpenStax, Human biology. OpenStax CNX. Dec 01, 2015 Download for free at http://legacy.cnx.org/content/col11903/1.3
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