haemoglobin composition and types pdf

Haemoglobin Composition And Types Pdf

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Hemoglobin in blood carries oxygen from the lungs or gills to the rest of the body i.

Hemoglobin has a critical role in your body. It's the protein in red blood cells RBCs that carries oxygen from your lungs to the tissues of your body. As such, abnormal levels of hemoglobin, or abnormal types of hemoglobin can result in serious disease. Let's look at the normal ranges of hemoglobin in adults in children, conditions that cause either a low hemoglobin or a high hemoglobin level, and the tests for and significance of hereditary abnormal hemoglobins.

Hemoglobin and its measurement

Hemoglobin has a critical role in your body. It's the protein in red blood cells RBCs that carries oxygen from your lungs to the tissues of your body. As such, abnormal levels of hemoglobin, or abnormal types of hemoglobin can result in serious disease. Let's look at the normal ranges of hemoglobin in adults in children, conditions that cause either a low hemoglobin or a high hemoglobin level, and the tests for and significance of hereditary abnormal hemoglobins.

Hemoglobin is protein in red blood cells that is made up of four chains. Each of these chains contains a compound known as heme, which in turn contains iron, which is what transports oxygen in the bloodstream. Hemoglobin is responsible for the shape of RBCs, which usually appear like donuts but with a thin center rather than a hole.

In conditions involving abnormal hemoglobin, such as sickle cell anemia, the abnormal shape of the RBCs can lead to problems. Hemoglobin functions by binding and transporting oxygen from the capillaries in the lungs to all of the tissues in the body.

It also plays a role in the transport of carbon dioxide from the tissues of the body back to the lungs. Nitric oxide and carbon monoxide are also able to bind with hemoglobin, with carbon monoxide binding much more readily than oxygen the reason why carbon monoxide poisoning is so serious. A low hemoglobin level is referred to as anemia. With RBCs, in turn, there may be:. The many possible causes of a low hemoglobin include:. Several conditions are associated with an elevated level of hemoglobin, including:.

In many of these, the increased level is a compensatory mechanism to try to supply more oxygen to the body. A hemoglobin level may be artificially elevated only appear to be elevated due to dehydration.

Hemoglobin may also be "normally" elevated in people living at high altitudes. Conditions in which hemoglobin has an abnormal structure include:. People with thalassemia often have life-long anemia and many require frequent transfusions. Thalassemia intermedia is also termed "non transfusion dependent thalassemia" and may not be discovered until adulthood. When a doctor notes a low hemoglobin level, they also looks at other lab tests that may help determine the cause.

These include:. Normal hemoglobin levels vary by age and sex. If you hear about hemoglobin, you may think of bleeding, especially heavy menstrual bleeding. Yet there is a wide range of disorders that can result in either an elevated or decreased hemoglobin. In addition, abnormal types of hemoglobin can contribute to disease. In order to determine a cause of a low or high hemoglobin, your doctor will ask questions, perform a physical exam, and look at other blood tests in combination with your hemoglobin level.

Limiting processed foods and red meats can help ward off cancer risk. These recipes focus on antioxidant-rich foods to better protect you and your loved ones. Sign up and get your guide! University of Rochester Medical Center. Health Encyclopedia. What Are Red Blood Cells? Measurement and interpretation of hemoglobin concentration in clinical and field settings: a narrative review. Ann N Y Acad Sci. Patient education: Anemia caused by low iron in adults Beyond the Basics.

Updated April 9, National Library of Medicine. Hemoglobin Test. Updated July 31, Updated August 24, RBC indices. Updated October 8, Table of Contents View All. Table of Contents. Low Hemoglobin. Elevated Hemoglobin. Abnormal Hemoglobin. Evaluating Levels.

The pigment in hemoglobin is responsible for the red color of blood. Recognizing Dehydration. Normal Hemoglobin Ranges Normal hemoglobin levels vary by age and sex. Adult male : What Are Blood Dyscrasias? Was this page helpful? Thanks for your feedback! Sign Up. What are your concerns? Article Sources. Verywell Health uses only high-quality sources, including peer-reviewed studies, to support the facts within our articles.

Read our editorial process to learn more about how we fact-check and keep our content accurate, reliable, and trustworthy. Related Articles. What Is a Normal Hemoglobin Level? Why Are My Fingernails Blue? Verywell Health uses cookies to provide you with a great user experience. By using Verywell Health, you accept our.

Hemoglobin Importance Within the Body

Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. High and low hematocrit Hct and hemoglobin Hb levels are associated with the risk of cardiovascular disease.

Methods for the measurement of hemoglobin Hb were first developed well over a century ago, so that hemoglobin was among the first diagnostic blood tests available to clinicians during the first decades of the 20th century when laboratory medicine was in its infancy. Today it is the most frequently requested blood test and is performed not only in the hospital laboratory but in a variety of healthcare settings, by a range of healthcare personnel, using technology of diverse sophistication. In an intensive care and emergency room setting, for example, hemoglobin is measured by nursing staff using technology incorporated into blood gas analyzers. The focus of this article is methods currently used to measure the blood concentration of hemoglobin c tHb both in the laboratory and beyond, but it begins with a brief consideration of the structure and function of hemoglobin and the clinical utility of c tHb measurement. Normal cell function depends on a continuous supply of oxygen. As oxygen is consumed during cell metabolism, carbon dioxide is produced. A principle function of blood is the delivery of oxygen O 2 , present in inspired air, from the lungs to every cell in the body and delivery of carbon dioxide CO 2 from cells to the lungs, for elimination from the body in expired air.

Hemoglobin , also spelled haemoglobin , iron -containing protein in the blood of many animals—in the red blood cells erythrocytes of vertebrates —that transports oxygen to the tissues. Hemoglobin forms an unstable reversible bond with oxygen. In the oxygenated state, it is called oxyhemoglobin and is bright red; in the reduced state, it is purplish blue. Hemoglobin develops in cells in the bone marrow that become red blood cells. When red cells die, hemoglobin is broken up: iron is salvaged, transported to the bone marrow by proteins called transferrins , and used again in the production of new red blood cells; the remainder of the hemoglobin forms the basis of bilirubin , a chemical that is excreted into the bile and gives the feces their characteristic yellow-brown colour.


Hemoglobin is a molecule inside the red blood cells of human blood. It has two parts: the heme and the globin. The heme contains iron and transports oxygen from the lungs to the tissues as well as takes carbon dioxide from the tissues to the lungs.

A hemoglobin abnormality is a variant form of hemoglobin that is often inherited and may cause a blood disorder hemoglobinopathy. Hemoglobin is the iron-containing protein compound within red blood cells that carries oxygen throughout the body. It is made up of heme, which is the iron-containing portion, and globin chains, which are proteins. The globin protein consists of chains of amino acids, the "building blocks" of proteins. There are several different types of globin chains, named alpha, beta, delta, and gamma.

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None of the amino acids are well suited to bind oxygen, so both of these proteins have an additional iron-containing group (heme) as part of their structure. (Figure​.


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