Haemoglobin(HB) is the red pigmented protein located in the erythrocytes, and consists of four subunits. The main function is the transportation of oxygen and carbon dioxide in the blood, besides that gives the red color to the blood, also maintains the shape of red blood cells and acts as buffer. The (HB) degradation accumulates physiologically active catabolites.
In normal adults, at least 96% of the (HB) is HbA. HbA is usually about 2.5 - 3 % of total HB. Fetal HB predominant during the fetal life and diminishes rapidly during the first year of postnatal life. Also (HB) concentration can be diminshed as a consequence of haemorrhage or hemolysis or as a result of impaired blood formation in the blood marrow.
The normal Range:
Newborns: 17 to 22 gm/dl
One week of age: 15 to 20 gm/dl
One month of age: 11 to 15 gm/dl
Children: 11 to 13 gm/dl
Adults males: 14 to 18 gm/dl
Adults females: 12 to 16 gm/dl
Men after middle age: 12.4 to 14.9 gm/dl
Women after middle age: 11.7 to 13.8 gm/dl
A low (HB) levels is referred to anemia or low blood count.
A high (HB) can be seen in people living at high altitudes and also in people who smoke. Dehydration produces a falsely high (HB) measurements that disappeares when proper fluid balance is restored.
The adult HB and fetal HB have α chains combined with β (Hb A, α2β2), δ (Hb A2, α2δ2), or γ chains (Hb F, α 2γ2), Each of the different globin chains is controlled by distinct genes; two genes exist for the α and γ chains and one for each of the other chains.
And that leads to be familiar with a Spectrum of Inherited Hemoglobin Disorders
Inherited hemoglobin disorders fall into two main groups: (1)
the structural hemoglobin variants and (2) the thalassemias, which
are caused by defective globin production. They all follow a
recessive form of inheritance.
Those with a single defective globin gene carriers or heterozygotes
are known to be symptomless. And if two carriers marry, a one in
four chance exists that each child they produce will receive
defective genes from each parent as they are homozygous for the
particular disorder.
Also The structural variants result mostly from single amino acid substitutions in the α or β chains. Often these are innocuous, but in some cases they may alter the stability or functional properties of the hemoglobin and lead to a clinical disorder.
The thalassemias are classified according to the ineffectively synthesized globin chains, and they're a group of hereditary conditions that associated with quantative (HB) deficiency.
Finally that's how (HB) tests is often used to check for anemia ,usually such as (1) hematocrit or (2) complete blood count (CBC). Used for screening, diagnosis or monitoring a number of conditions and diseases that affect red blood cells (RBCs) and/or the amount of hemoglobin in blood.
how haemoglobin spectrum can be used to diagnose disorders in blood chemistry?
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