How to use Hemoglobin in a sentence
There is a reduction in cardiac output and an increase in hemoglobin oxygen affinity.
If you are anemic, you have too little hemoglobin because you have too few red blood cells.
The abnormal form of hemoglobin causes the red cells to become sickle-shaped.
Straw, pink, yellow, or amber pigments (xanthochromia) are abnormal and indicate the presence of bilirubin, hemoglobin, red blood cells, or increased protein.
People with sickle cell anaemia have sickle hemoglobin (HbS) which is different from the normal hemoglobin (HbA).Advertisement
Sickle cell anemia is usually inherited from parents who are carriers, who have the sickle cell trait-a milder form of sickle cell anemia, or one abnormal hemoglobin.
Sickle cell anemia is caused by an error in the gene that signals the body how to make hemoglobin.
The defective gene tells the body to make the abnormal hemoglobin HbS instead of the normal HbA, and this results in deformed red blood cells.
The error in the hemoglobin gene is due to a genetic mutation that occurred many thousands of years ago in people living in Africa, the Mediterranean basin, the Middle East, and India.
For children who are not tested, an electrophoresis test of the blood can detect the abnormal hemoglobin of sickle cell anemia.Advertisement
This test measures the speed at which a molecule moves in a gel and can detect abnormal hemoglobin HbS.
Drug research is focused on identifying drugs, such as hydroxyurea, that can increase the level of fetal hemoglobin in the blood.
Fetal hemoglobin is a form of hemoglobin that all humans produce before birth, but most stop producing it after birth.
Fetal hemoglobin seems to prevent "sickling" of red cells, and cells containing fetal hemoglobin tend to survive longer in the bloodstream.
Butyrate, a substance widely used as a food additive, was also being investigated as of 2004 as an agent that may increase fetal hemoglobin production.Advertisement
If one partner has sickle cell trait and the other does not, their children each have a 50 percent chance of having the sickle cell trait, and a 50 percent chance of having normal hemoglobin.
Sickle cell trait-Condition that occurs in people who have one of two possible genes responsible for the abnormal hemoglobin of sickle cell anemia.
H. "Therapies to increase fetal hemoglobin in sickle cell disease."
Based on results of this study, the American Diabetes Association (ADA) recommends routine glycated hemoglobin testing to measure long-term control of blood sugar.
The glycated (glycosylated) hemoglobin test is used to monitor the effectiveness of diabetes treatment.Advertisement
Glycated hemoglobin is a test that indicates how much glucose was in a person's blood during a two- to three-month window beginning about four weeks prior to sampling.
The normal range for glycated hemoglobin measured as HbA 1c is 3 to 6 percent.
Splenectomy can result in an increase and hemolytic anemia can result in a decrease in glycated hemoglobin.
Glycated hemoglobin-A test that measures the amount of hemoglobin bound to glucose.
Hemoglobin is an iron-containing protein that resides within the red blood cells.Advertisement
A very small fraction of hemoglobin spontaneously oxidizes per day, producing a protein of a slightly different structure called methemoglobin.
Poisoning by nitrite (or nitrate after its conversion to nitrite) results in the inability of hemoglobin to carry oxygen throughout the body.
Adverse symptoms occur when over 30 percent of the hemoglobin has been converted to methemoglobin.
Methemoglobin-A compound formed from hemoglobin by oxidation of its iron component.
The porphyrias are disorders in which the body produces too much porphyrin and insufficient heme (an iron-containing nonprotein portion of the hemoglobin molecule).
In immature red blood cells, heme is the featured component of hemoglobin.
Hemoglobin is the red pigment that gives red blood cells their characteristic color and their essential ability to transport oxygen.
Heme-The iron-containing molecule in hemoglobin that serves as the site for oxygen binding.
Porphyrin-An organic compound found in living things that founds the foundation structure for hemoglobin, chlorophyll, and other respiratory pigments.
Protoporphyrin-A kind of porphyrin that links with iron to form the heme of hemoglobin.
Iron is essential for the formation of hemoglobin, the chemical in the blood that carries oxygen to the cells.
Anemia in newborn infants is noted when hemoglobin levels are lower than expected for the birth weight and postnatal age.
Premature or low birth-weight infants may have lower hemoglobin levels.
It must be noted, however, that hemoglobin decreases naturally (physiologic decrease) in infants by eight to 12 weeks of age, leveling at a normal value of 11 g/dL or better.
An inherited form of hemolytic anemia, thalassemia comes from the production of abnormal hemoglobin.
It is characterized by low hemoglobin and unusually small and fragile RBCs (microcytosis), although the RBC count may be normal.
Thalassemia has several types that involve imbalances in the four chains of amino acids that comprise hemoglobin (alpha- and beta-globins).
In thalassemia minor, fetal hemoglobin (HbF), the hemoglobin form that circulates in the fetus, does not decrease normally after birth and may remain high in later life.
It is known as beta-thalassemia, because of an imbalance in the beta chain amino acids of hemoglobin.
Hemoglobin H disease is another form of thalassemia in which three of the four beta-globin genes are missing.
Sickle cell anemia is an inherited, chronic, incurable blood disorder that causes the body to produce defective hemoglobin, the abnormal HgbS, which occurs primarily in African Americans.
Unlike normal oval cells, fragile sickle cells cannot hold enough hemoglobin to nourish body tissues.
Sources of iron such as liver, red meat, whole grains, and poultry may help maintain hemoglobin levels and reduce the likelihood of deficiency-related anemias.
Megaloblast-A large erythroblast (a red marrow cell that synthesizes hemoglobin).
Red blood cells-Cells that carry hemoglobin (the molecule that transports oxygen) and help remove wastes from tissues throughout the body.
Thalassemia describes a group of inherited disorders characterized by reduced or absent amounts of hemoglobin.
Hemoglobin is the protein in red blood cells that carries oxygen throughout the body.
In all types of thalassemia, the quantity of hemoglobin produced is reduced or absent.
Although both alpha and beta thalassemias affect hemoglobin, these diseases affect the body in distinctly different ways.
Individuals with hemoglobin H disease have inherited one completely defective gene and one gene that has one rather than two functional loci.
As a result, individuals with hemoglobin H disease can experience events of hemolytic anemia-anemia caused by the rapid breakdown of the red blood cells.
Hemoglobin H disease is milder than alpha thalassemia and usually milder than beta thalassemia.
Alpha thalassemia major, sometimes called hemoglobin Barts or hydrops fetalis, is a fatal disease that results in severe anemia that begins even before birth.
It is caused by a change in the gene for the beta globin component of hemoglobin.
Beta thalassemia minor describes a disease where only one gene of the pair that control beta hemoglobin production is defective.
Despite this estimate, the number of babies born with hemoglobin H disease or alpha thalassemia major is very low.
However, at least one state, California, has observed growing hemoglobin H disease rates that are high enough to justify universal newborn screening for the condition.
Humans normally make several types of hemoglobin.
Alpha globin is also a component of fetal hemoglobin.
Hemoglobin H symptoms can also be a part of a unique condition called alpha thalassemia mental retardation syndrome.
Most individuals have two normal copies of the beta globin gene, which is located on chromosome 11 and makes the beta globin component of normal adult hemoglobin.
Hemoglobin H disease is a relatively mild form of thalassemia that may go unrecognized.
Education is an important part of managing the health of an individual with hemoglobin H disease.
For many individuals with hemoglobin H disease, this is rarely required.
Because alpha globin is a necessary component of hemoglobin, absence of all functioning alpha globin genes leads to serious medical consequences that begin even before birth.
However, this effort is ineffective without the needed genetic instructions to make enough functioning hemoglobin.
A complete blood count will identify low levels of hemoglobin, small red blood cells, and other red blood cell abnormalities that are characteristic of a thalassemia diagnosis.
Hemoglobin electrophoresis is a test that can help identify the types and quantities of hemoglobin made by an individual.
They can be used instead of or in various combinations with hemoglobin electrophoresis to determine the types and quantities of hemoglobin present.
Hemoglobin electrophoresis results are usually within the normal range for all types of alpha thalassemia.
Other possible treatments may include gene therapy techniques aimed at increasing the amount of normal hemoglobin the body is able to make.
Individuals with hemoglobin H disease can reduce the likelihood of symptoms by avoiding infections and certain environmental triggers.
If parents are thinking of having a child and believe they might be carriers of defective hemoglobin genes, they can be screened and receive genetic counseling so that they can assess their options.
Globin-One of the component protein molecules found in hemoglobin.
Normal adult hemoglobin has a pair each of alpha-globin and beta-globin molecules.
Hemoglobin A-Normal adult hemoglobin that contains a heme molecule, two alpha-globin molecules, and two beta-globin molecules.
Hemoglobin electrophoresis-A laboratory test that separates molecules based on their size, shape, or electrical charge.
Hydroxyurea-A drug that has been shown to induce production of fetal hemoglobin.
Fetal hemoglobin has a pair of gamma-globin molecules in place of the typical beta-globins of adult hemoglobin.
Higher-than-normal levels of fetal hemoglobin can ameliorate some of the symptoms of thalassemia.
Red blood cell-Cells that carry hemoglobin (the molecule that transports oxygen) and help remove wastes from tissues throughout the body.
Other supportive data include measuring levels of factors V and VIII, fibrinogen, hemoglobin, and platelets, any of which may be diminished or entirely depleted.
A fetal hemoglobin test (Hgb electrophoresis) measures the level of fetal hemoglobin (Hemoglobin F or HbF) in the blood of infants and children.
Fetal hemoglobin, an alkali-resistant form of hemoglobin, is the major hemoglobin component in the bloodstream of the fetus.
Fetal hemoglobin is one of six types of hemoglobin measured in the clinical laboratory by a method called hemoglobin electrophoresis.
The determination of fetal hemoglobin in the blood of infants and children identifies normal and abnormal levels, defining what percentage of total hemoglobin is made up of fetal hemoglobin.
Knowing this level may help doctors evaluate low concentrations of normal hemoglobin in red blood cells (anemia), as well as higher-than-normal levels of fetal hemoglobin or its hereditary persistence.
Fetal hemoglobin measurement helps diagnose a group of inherited disorders that affect hemoglobin production, among which are the thalassemias and sickle cell anemia.
Hemoglobin is the oxygen-carrying protein in red blood cells.
Red blood cells deliver hemoglobin throughout the body, ensuring that all body tissues have the oxygen they need for life and proper function.
Hemoglobin consists primarily of iron-bearing proteins called heme groups and moiety globin protein, which together give hemoglobin its ability to carry oxygen.
Among the six types of hemoglobin, HbA is the normal adult hemoglobin, and HbF is the major fetal hemoglobin.
All types of hemoglobin are electrically charged, which enables them to be identified and quantified in the laboratory by hemoglobin electrophoresis techniques.
At birth, the newborn's blood is composed of about 70 percent fetal hemoglobin.
As the infant's bone marrow begins to produce new red cells, fetal hemoglobin begins to decrease rapidly.
Normally, only 2 percent or less of total hemoglobin is found as fetal hemoglobin after six months and throughout childhood; in adulthood, only traces (0.5% or less) are found in total hemoglobin.
In some diseases associated with abnormal hemoglobin production (hemoglobinopathy), fetal hemoglobin may persist in larger amounts.
When this occurs, the increased amounts of fetal hemoglobin raise questions of possible underlying dysfunction or disease.
Defects in hemoglobin production may be either genetic or acquired.
Testing for levels of fetal hemoglobin and other types of hemoglobin may be a first, important step in the investigation of possible hemoglobinopathies.
No preparation is needed before performing fetal hemoglobin tests, and fasting (nothing to eat or drink for a period of hours before the test) is not required.
Hemoglobinopathy-A disorder of hemoglobin, which can be either the presence of abnormal types of hemoglobin or abnormal levels of specific types of hemoglobin.
The oxygen is then picked up by hemoglobin, the oxygen-carrying protein in red blood cells, and delivered throughout the body through the circulatory system.
Normally when a person breathes fresh air into the lungs, the oxygen in the air binds with a molecule called hemoglobin (Hb) that is found in red blood cells.
Because the oxygen binding process is reversible, hemoglobin can be used over and over again to pick up oxygen and move it throughout the body.
In the lungs, CO competes with oxygen to bind with the hemoglobin molecule.
Hemoglobin prefers CO to oxygen and accepts it more than 200 times more readily than it accepts oxygen.
Not only does the hemoglobin prefer CO, it holds on to the CO much more tightly, forming a complex called carboxyhemoglobin (COHb).
As a person breathes CO contaminated air, more and more oxygen transportation sites on the hemoglobin molecules become blocked by CO.
Heavy smokers can start off with up to 9 percent of their hemoglobin already bound to CO, which they regularly inhale in cigarette smoke.
This blood test measures the amount of CO that is bound to hemoglobin in the body.
The half-life of CO in normal room air is four to five hours, which means that in four to five hours half of the CO bound to hemoglobin will be replaced with oxygen.
When examined under a microscope, the RBCs also appear pale or light colored from the absence of heme, the major component of hemoglobin, which is the iron-bearing protein and coloring pigment in RBCs.
It is an important component of hemoglobin and myoglobin, the type of hemoglobin in muscle tissue.
Diagnostic testing starts with a complete blood count (CBC) and differential, counting RBCs, white blood cells (WBCs) and measuring hemoglobin (Hgb), hematocrit (Hct), and other factors.
In iron deficiency anemia, the RBC count can be normal or elevated and hemoglobin will be abnormally low.
In infants, iron deficiency anemia is defined as having a hemoglobin level below 109 mg/ml when measured in whole blood, and a hematocrit of less than 33 percent.
Different types of hemoglobin may be measured by a diagnostic testing method called hemoglobin electrophoresis.
Protoporphyrin IX, a component of hemoglobin, may be measured to help confirm a diagnosis of iron deficiency anemia.
The diagnosis of iron deficiency anemia may include a test for oral iron absorption, especially when evidence suggests that oral iron supplements have failed to raise hemoglobin.
Red meat sources reliably replace the heme component of red blood cells, raising hemoglobin levels and helping to correct iron deficiency.
Hemoglobin consists of a complex of a protein plus heme.
Normally, during the course of red blood cell formation, protoporphyrin IX acquires iron, to generate heme, and the heme becomes incorporated into hemoglobin.
Iron-critical in the production of hemoglobin, the oxygen-carrying protein in red blood cells, and myoglobin found in muscle tissue.
Iron deficiency causes anemia (low hemoglobin and reduced numbers of red blood cells), which results in tiredness and shortness of breath because of poor oxygen delivery.
Anemia-A lack of hemoglobin, the compound in blood that carries oxygen from the lungs throughout the body and brings waste carbon dioxide from the cells to the lungs, where it is released.
Measurements needed to calculate indices are the red blood cell count, hemoglobin, and hematocrit.
The average amount of hemoglobin inside an RBC expressed in picograms.
The MCH is calculated by dividing the hemoglobin concentration in grams per deciliter by the RBC count in millions per microliter, then multiplying by 10.
The average concentration of hemoglobin in the RBCs expressed as a percent.
It is calculated by dividing the hemoglobin in grams per deciliter by the hematocrit, then multiplying by 100.
Healthy people have an adequate number of correctly sized red blood cells containing enough hemoglobin to carry sufficient oxygen to all the body's tissues.
Anemia is diagnosed when either the hemoglobin or hematocrit of a blood sample is too low.
Failure to produce hemoglobin results in smaller than normal cells.
The RBC count is low, but the size and amount of hemoglobin in the cells are normal.
A low MCH indicates that cells have too little hemoglobin.
This is caused by deficient hemoglobin production.
The MCHC is the ratio of hemoglobin mass in the RBC to cell volume.
Cells with too little hemoglobin are lighter in color and have a low MCHC.
Hypochromic-A descriptive term applied to a red blood cell with a decreased concentration of hemoglobin.
Mean corpuscular hemoglobin concentration (MCHC)-A measurement of the average concentration of hemoglobin in a red blood cell.
Mean corpuscular hemoglobin (MCH)-A measurement of the average weight of hemoglobin in a red blood cell.
Normochromic-A descriptive term applied to a red blood cell with a normal concentration of hemoglobin.
Red blood cell indices-Measurements that describe the size and hemoglobin content of red blood cells.
As the blood flow increases, the amount of deoxyhemoglobin, a form of hemoglobin that has lost its oxygen content, decreases in the affected area of the brain.
If a blood test reveals low hemoglobin, supplementation with iron may be recommended.
The destroyed red blood cells release the blood's red pigment (hemoglobin) which degrades into a yellow substance called bilirubin.
Bilirubin is a yellow-orange bile pigment produced during the breakdown of hemoglobin, the iron-bearing and oxygen-carrying protein in red blood cells.
This situation results in jaundice in over 60 percent of newborns, usually due to the presence of fetal hemoglobin released into the blood during the normal destruction of fetal red blood cells.
Copper supports hemoglobin, which brings an adequate supply of blood to the hair shaft.
Every time you donate blood, your blood pressure and temperature are taken, not to mention pulse and hemoglobin rate.
Once inhaled, carbon monoxide combines with oxygen carrying hemoglobin to form carboxyhemoglobin.
In the late 1930s Max Perutz used the technique to study hemoglobin and the enzyme chymotrypsin.
In the survey, 3% of men and 8% of women had a hemoglobin concentration below these limits indicating anemia.
A normal hemoglobin molecule contains two alpha globin molecule contains two alpha globins and two beta globins to make up the complement of 4 globins.
Human adult hemoglobin is actually a composite of four protein chains called globin is actually a composite of four protein chains called globins, knotted around each other.
This has the effect of reducing the number of red cells, which are full of the iron-containing protein hemoglobin.
Those with the lowest baseline hemoglobin had the greatest increase in hemoglobin.
They also had slight decreases in glycosylated hemoglobin, a measure of chronically high blood glucose levels.
Measured total hemoglobin Direct measurement of total hemoglobin provides more accurate results for bypass patients.
Biomimetic sensors utilize a material that mimics the response of human hemoglobin to carbon monoxide.
Investigations Children presenting with an acute pulmonary bleed will have a reduced hemoglobin and widespread bilateral infiltrates on chest x-ray.
These bicarbonate ions immediately latch onto a section of the crocodiles ' hemoglobin molecules, forcing the hemoglobin to release its attached oxygen.
To simplify notation we define,, ,, ,, ,, , and the total hemoglobin in all forms.
This reduces the oxygen carrying capacity of hemoglobin and the amount of oxygen reaching the periphery is decreased.
There is either an excess release or incomplete removal of the bile pigment derived from hemoglobin in red blood cells.
The venous oxygen saturation measures what percentage of hemoglobin in the vein is carrying oxygen.
Without iron the hemoglobin molecules cannot carry oxygen and the tissues of the body become oxygen starved.
An increase in hemoglobin content increases the stickiness or viscosity of the blood as it flows around the body.
So instead of normally having 100% of the hemoglobin saturated with oxygen, smokers are down to about 85% of normal.
If an individual inherits one sickle hemoglobin gene they generally have no symptoms but they can pass this gene on to their children.
People with gastrointestinal disorders should also be mindful of their iron intake, as their condition may cause iron to be absorbed into the small intestine, thus taking away the amount available for hemoglobin.
As the parasites mature, they block the blood flow and can lead to anemia (reduced hemoglobin) or heart failure.
Bilirubin is a breakdown product of hemoglobin (the red chemical in blood that carries oxygen).
Carbon monoxide causes death by binding with hemoglobin that would normally transport oxygen throughout the body.
Sickle cell anemia-An inherited disorder in which red blood cells contain an abnormal form of hemoglobin, a protein that carries oxygen.
Heme (component of hemoglobin in red blood cells that carries oxygen throughout the body) is broken down into bilirubin, which moves to the liver where it is processed and added to bile, a digestive fluid.
As the cells are destroyed, hemoglobin, the component of red blood cells which carries the oxygen, is liberated.
Sickle cell anemia, also called sickle cell disease (SS disease), is an inherited condition caused by having abnormal hemoglobin, the protein that carries oxygen in the blood.
Children with sickle cell anemia produce two abnormal hemoglobin proteins (inheriting one from each parent), which makes their red blood cells easily destructible while giving them a sickle-like shape.
Since the red blood cells do not have a normal shape, their circulation in the small blood vessels is impaired as well as the function of the abnormal hemoglobin (HbS) which can no longer carry oxygen with maximum efficiency.
Anemia is a blood disorder characterized by abnormally low levels of healthy red blood cells (RBCs) or reduced hemoglobin (Hgb), the iron-bearing protein in red blood cells that delivers oxygen to tissues throughout the body.
Affected individuals have mild hemoglobin H disease, mild-to-moderate mental retardation, and characteristic facial features, as well as various other developmental processes that mimic hemoglobin H disease.
Hemoglobin electrophoresis can also detect structurally abnormal hemoglobins that may be co-inherited with a thalassemia trait.
Testing for fetal hemoglobin requires that a blood sample be drawn from the child.
Anemia is a blood disorder characterized by abnormally low levels of healthy RBCs or reduced levels of hemoglobin (Hgb), the iron-bearing protein in RBCs that delivers oxygen to tissues throughout the body.
It has been observed that some children with sickle cell anemia continue to produce large amounts of fetal hemoglobin after birth, and studies have shown that these children have less severe cases of the disease.
Diagnosing thalassemia and sickle cell anemia, both of which involve disorders of hemoglobin, will require measuring the different types of hemoglobin through a laboratory testing method called hemoglobin electrophoresis.
The ADA recommends that glycated hemoglobin testing be performed during a person's first diabetes evaluation, again after treatment is begun and glucose levels are stabilized, then repeated semiannually.