Hemoglobin H disease is a type of Thalassemia.
Thalassemia is a genetic (inherited) disorder, affecting the haemoglobin's structure, more precisely, the protein chains of the haemoglobin, which are responsible for carrying the oxygen and carbon dioxide inside the Red Blood Cells. If any of these protein chains is defective, the haemoglobin's ability to bind to (carry) the oxygen/carbon dioxide is hindered.
The two kind of protein chains are:
Beta globin chain = needs one gene per parent, and
Alpha globin chain = needs two genes per parent.
In Hemoglobin H disease the Alpha globin chains are affected, namely, three genes (one from one parent and 2 from the other parent) are defective (missing). That results in insufficiant oxygenation of the tissues, - anaemia -, ranging from moderate to severe.
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A : Hb H is Hemoglobin H, which is a type of hemoglobin which is normally found in adult human beings. Hemoglobin is the oxygen-carrying chemical compound in our red blood cell.
The importance of hemoglobin for erythrocyte function is that it gives them oxygen carrying abilities. Without hemoglobin, the erythrocyte would be unable to carry and transport oxygen where it needs to go.
Hemoglobin and Hemocrit levels
Hemoglobin contain C, H, O, N, Fe.
The medical abbreviation "H and H" usually stands for hemoglobin and hematocrit levels. Hemoglobin measures how much oxygen-carrying protein is present in the blood, while hematocrit measures the proportion of red blood cells to the total blood volume. These values are important for understanding a person's blood health.
H. Lehmann has written: 'Human haemoglobin variants and their characteristics' -- subject(s): Hemoglobin, Tables 'Man's haemoglobins' -- subject(s): Hemoglobin, Hemoglobinopathy
hemoglobin is reduced when the boby is lacking iron which is responsible for the formation of hemoglobin
H stands for "Hemoglobin" which resides in the blood. and ism stands for "International safety management"
H H. Jaffe has written: 'The importance in antibonding orbitals'
The Cl- entering the RBC from the chloride shift does not combine with free H+ ions to form HCl because those H+ ions bind with hemoglobin instead. As such, hemoglobin acts as a buffer.
L. H. B. Wallett has written: 'Human haemoglobin variants and their identification' -- subject(s): Hemoglobin, Hemoglobins
the primary factor in oxygen attachment to, or from, hemoglobin is the partial pressure of oxygen. actively metabolized cells will use oxygen in energy production thus enhancing oxygen release from hemoglobin to meet their energy production requirements.