This is due to a decreased total carrying capacity, such as a reduced Hemoglobin content.

Hemoglobin (; also spelled haemoglobin and abbreviated Hb or Hgb ) is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates ( with the exception of the fish family Channichthyidae ) as well as the tissues of some invertebrates.

Hemoglobin is involved in the transport of other gases: it carries some of the body's respiratory carbon dioxide ( about 10 % of the total ) as carbaminohemoglobin, in which CO < sub > 2 </ sub > is bound to the globin protein.

Hemoglobin is also found outside red blood cells and their progenitor lines.

Hemoglobin ( Hb ) is synthesized in a complex series of steps.

Hemoglobin binding affinity for CO is 250 times greater than its affinity for oxygen, meaning that small amounts of CO dramatically reduce hemoglobin's ability to transport oxygen.

Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening.

* Hemoglobin F ( α < sub > 2 </ sub > γ < sub > 2 </ sub >)-In adults Hemoglobin F is restricted to a limited population of red cells called F-cells.

Hemoglobin deficiency is, in general, strictly distinguished from hypoxemia, defined as decreased partial pressure of oxygen in blood, although both are causes of hypoxia ( insufficient oxygen supply to tissues ).

Hemoglobin concentration measurement is among the most commonly performed blood tests, usually as part of a complete blood count.

* Hemoglobin A1C ( HbA1c ) – Hemoglobin is the substance in red blood cells that carries oxygen to the cells.

Hemoglobin in the erythrocytes also carries some of the waste product carbon dioxide back from the tissues ; most waste carbon dioxide, however, is transported back to the pulmonary capillaries of the lungs as bicarbonate ( HCO < sub > 3 </ sub >< sup >-</ sup >) dissolved in the blood plasma.

Hemoglobin ( the main component of red blood cells ) is an iron-containing protein that facilitates transportation of oxygen and other respiratory gases to tissues.

Hemoglobin and Myoglobin are examples of hemeprotein that are essential in the storing and transports of oxygen in mammals. Hemoglobin is a quaternary protein that occurs in the red blood cell, whereas, myoglobin is a tertiary protein found the muscle cells of mammals.

Hemoglobin, which is the principal oxygen carrier in humans has four sub-units in which the iron ( II ) ion is coordinated by the planar, macrocyclic ligand protoporphyrin IX ( PIX ) and the imidazole nitrogen atom of a histidine residue.

Hemoglobin is a protein found in red blood cells, and is responsible for the transportation of oxygen through the body .< ref > Connie C. W.

Hemoglobin in the blood carries oxygen from the respiratory organs ( lungs or gills ) to the rest of the body ( i. e. the tissues ) where it releases the oxygen to burn nutrients to provide energy to power the functions of the organism, and collects the resultant carbon dioxide to bring it back to the respiratory organs to be dispensed from the organism.

Hemoglobin has an oxygen binding capacity of 1. 34 ml O < sub > 2 </ sub > per gram of hemoglobin, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood.

In general, hemoglobin can be saturated with oxygen molecules ( oxyhemoglobin ), or desaturated with oxygen molecules ( deoxyhemoglobin ).< ref >" Hemoglobin Home.

Hemoglobin can bind protons and carbon dioxide, which causes a conformational change in the protein and facilitates the release of oxygen.

Hemoglobin deficiency can be caused either by decreased amount of hemoglobin molecules, as in anemia, or by decreased ability of each molecule to bind oxygen at the same partial pressure of oxygen.

Hemoglobin, the oxygen transporting protein found in red blood cells

Hemoglobin binds oxygen cooperatively due to steric conformation changes in the protein complex, which increases hemoglobin's affinity for oxygen when partially oxygenated.

Hemoglobin differs in how it responds to magnetic fields, depending on whether it has a bound oxygen molecule.

Hemoglobin binds to carbon monoxide preferentially compared to oxygen ( approx 240: 1 ), so effectively, COHb will not release the carbon monoxide, and therefore hemoglobin will not be available to transport oxygen from the lungs to the rest of the body.

Hemoglobin consists mostly of protein subunits ( the " globin " chains ), and these proteins, in turn, are folded chains of a large number of different amino acids called polypeptides.

Hydrogen bonds stabilize the helical sections inside this protein, causing attractions within the molecule, folding each polypeptide chain into a specific shape .< ref >" Hemoglobin Tutorial.

One protein being investigated at the time was Hemoglobin.

There are two subunits that make up the hemoglobin protein: beta-globins and alpha-globins .< ref >- Hemoglobin, Beta-Genetics Home Reference.

Here is how some of the 192 domains of the " Hemoglobin, alpha-chain from Human ( Homo sapiens )" protein are displayed.

Hemoglobin ( Hb ) is the iron-containing protein that binds oxygen in red blood cells.

This porphyrin ring consists of four pyrrole molecules cyclically linked together ( by methene bridges ) with the iron ion bound in the center .< ref >" Hemoglobin.

* Hemoglobin A ( α < sub > 2 </ sub > β < sub > 2 </ sub >) ()-The most common with a normal amount over 95 %

* Hemoglobin S ( α < sub > 2 </ sub > β < sup > S </ sup >< sub > 2 </ sub >)-A variant form of hemoglobin found in people with sickle cell disease.

* Hemoglobin AS-A heterozygous form causing Sickle cell trait with one adult gene and one sickle cell disease gene

* Hemoglobin SC disease-A compound heterozygous form with one sickle gene and another encoding Hemoglobin C.

This supports tighter control over blood sugar and Hemoglobin A1c levels, reducing the chance of long-term complications associated with diabetes.

Hemoglobin reacts with blood glucose in various ways ; the HbA1c sub-type reacts irreversibly.

One randomized controlled trial found that self-monitoring of blood glucose did not improve the HbA1c among " reasonably well controlled non-insulin treated patients with type 2 diabetes ". A recent meta-analysis of 47 randomized controlled trials encompassing 7677 patients showed that self-care management intervention improves glycemic control in Diabetics, with an estimated 0. 36 % ( 95 % CI, 0. 21-0. 51 ) reduction in their glycosylated Hemoglobin values .< ref > Minet, L., Moller, S., Vach, W., Wagner, L., & Henriksen, J. E. ( 2010 ).

Hemoglobin mutants with weaker cooperativity may exhibit a reduced Bohr effect.

These target cells ( from red blood cells ) are associated with Hemoglobin C ( HbC ) disease, Asplenia, Liver Disease, Thalassemia and severe Iron deficiency anemia.

## Hemoglobin H Inclusions-alpha thalassemia, greenish-blue inclusion bodies appear in many erythrocytes after four drops of blood is incubated with 0. 5mL of Brilliant cresyl blue for 20 minutes at 37 ° C.