Sickle Cell Disease: Haemoglobin

The red blood cells have an unusual structure compared to other cells in the human body, as it lacks a nucleus, mitochondria or endoplasmic reticulum (###). However, the enzyme component in the red blood cells allow it to produce small amount of energy (ATP from glucose). The mature red cell contains about 34 percent haemoglobin (a complex iron bearing pigment that transports oxygen). It gives a red colour to the cell, with a combination of heme and globin (###). Haemoglobin is the functional component of the cell, contained in the interior of the cell, and the outer surface of the cell is surrounded by a cell membrane. It has a pale, greenish yellowish appearance when unstained, and reversibly combined with oxygen and, to a lesser extent with carbon dioxide (###). The average concentration of haemoglobin is 14 g/100 ml blood in women and 16 g/100 ml in men (###). The production of the erythrocytes, occur primarily in the red marrow of the spongy bones. The vast surface area is important in the transport of oxygen from the lungs to the tissue because of quick exchange of oxygen in both sites that occurs across the red cell surface (@@@). An adult female has approximately 4.8 million/cu mm red cells, and adult male has approximately 5.5 million/cu mm red cells. An erythrocyte can stay between 80 to 120 days in

Sickle cell disease, also known as SCD, is a hereditary blood disorder that takes place due to mutation in the hemoglobin gene that is found in red blood cells. While it is said to have originated in Africa and is mostly predominant in African Americans, sickle cell disease is now common among different ethnic groups all over the world. Sickle cell anemia (HbSS) infects “an estimated 70,000 to 100,000 Americans”(Housman) and accounts for approximately 70% of anemia in the United States. Hemoglobin functions as an oxygen carrying protein as it carries oxygen from the lungs through the arteries and to the rest of the body. In sickle cell disease,

Now, what is sickle cell? Sickle cell anemia also known as sickle cell disease is an inherited blood disease that cause blood cells to form in crescent shape at low oxygen levels. “ sickle cell is a group of disorders that affects hemoglobin.” ( genetics home reference) Sickle cell is a very important and life threatening disease that can lead to a challenging life. Instead of moving brought the blood stream easy sickle cells can get clogged up in blood vessels and when this occurs the body's organs can not get the appropriate amount of oxygen needed.

The binding of oxygen to hemoglobin is cooperative. This means that once an oxygen molecule is bound to an iron of one of the four heme groups of deoxygenated hemoglobin, the affinity of the resulting oxygenated hemoglobin molecule towards oxygen will be greater than that of the starting deoxygenated hemoglobin. As a result, the binding of a second oxygen molecule

Abnormal haemoglobin, known as haemoglobin S, is the cause of sickle cell disease. The problem in haemoglobin S is caused by a small defect in the gene that directs the production of the beta globin part of haemoglobin, which changes the way that haemoglobin is meant to work. People who have SCD have inherited two abnormal haemoglobin genes, one from each parent. In all forms of the disease, at least one of the two abnormal genes causes the body to create haemoglobin S. When someone has two haemoglobin S genes, haemoglobin SS, the disease is called sickle cell anaemia. This is the most common and also most severe type of SCD.

Haemoglobin determination, or haemoglobinometry, is the measurement of the concentration of haemoglobin in the blood. Haemoglobin's main function in the body is to carry oxygen from the lungs to the tissues and to assist in transporting carbon dioxide from the tissues to the lungs. The formation of haemoglobin takes place in the developing red cells located in bone marrow. Haemoglobin values are affected by age, sex, pregnancy, disease, and altitude.

Sickle Cell Disease is an inherited blood disorder that affects the red blood cells. The red blood cells that turns normal red blood cells that are healthy and functioning into cells that are shaped sickled and crescent moon form become severely low and anemic. The oxygen - carry molecule in red blood cells that are called hemoglobin that creates an error in the red blood cell, that makes the cell sickled. When the sickled shaped cells block small vessels the condition results in oxygen depletion to the tissues surrounding the blocked vessels, Which the damages tissues causes many health

1) Sickle Cell Disease (SCD) (Sickle Cell Crisis): Sickle cell disease is a hereditary disease. The majority of individuals affected by SCD are those of African descent (Yawn & John-Sowah, 2015). SCD develops hereditarily by an individual being homozygous for sickle hemoglobin (HbSS) (Yawn & John-Sowah, 2015). Individuals will also have another abnormal hemoglobin gene, such as HbSC (Yawn & John-Sowah, 2015). The red blood cells (RBCs) in SCD lose oxygen and become sickled (Yawn & John-Sowah, 2015). The RBCs loose flexibility and shape; sickled cells have been described as having a crescent moon shape (Yawn & John-Sowah, 2015). Organ and tissue damage is due to the sickled RBCs (Rees & Gibson, 2011). Without flexibility, the sickled cells cause vaso-occlusions which lead to tissue infarction and inflammation (Rees & Gibson, 2011). Vasoocclusive crisis (VOC) is a common complication of SCD that will be sudden and severe causing severe pain (Yawn & John-Sowah, 2015). Individuals must be monitored for infection, pain, renal failure, cerebrovascular disease, and acute chest syndrome (Rees & Gibson, 2011). Individuals with SCD are at a high risk for stroke (Yawn & John-Sowah, 2015).

Oxygen is not very soluble in an aqueous solution such as blood so it needs to bind to hemoglobin in order to be transported. Each of hemoglobin iron ions can bind to one oxygen molecule which means that hemoglobin can carry four oxygen molecules at a time. The reason why oxygen binding to hemoglobin is very efficient is because of a process called “cooperative” binding.

Sickle Cell Disease (SCD) sickle shaped red blood cells are abnormal in size and function; compared to the Thalassemias red blood cells appear normal in appearance but there are not enough of them being produced for the body to sustain homeostasis. The two diseases have basic similarities within their diagnosis and treatments. They differ in the way of which, SCD complications exceed Thalassemias, with Thalassemias epidemiology reaching more ethnic backgrounds and numbers affected over a greater geographical area.

Alpha hemoglobin have two identical gene, which are called alpha hemoglobin 1 gene and alpha hemoglobin 2, which gives instructions on the production of a protein called alpha-globin. Alpha-globin is a piece of a large protein called hemoglobin. Hemoglobin molecule is a complex of two alpha chains and two beta chains and is a primary part of red blood cell cytoplasm and transport molecular oxygen from the lungs to the tissue and return carbon dioxide to the lungs. It is composed of two identical globin chains, which transports heme molecules and heme molecules are needed for red blood cells to pick up oxygen in the lungs and deliver it to the body’s tissues. In this report, I analyze the homology of alpha hemoglobin of human (Homo sapiens),

23. Describe the structural-molecular biochemistry changes that occur in hemoglobin that occur when oxygen binds to hemoglobin

The reason red blood cells are capable of doing this is due to the Haemoglobin. The Haemoglobin is a protein inside the red blood cell that carries oxygen. Red blood cells are made in the bone marrow and from there travel throughout the bloodstream.

-Due to the formal charges of oxygen, pi-backbonding plays a very minor role in the bonding of oxygen to hemoglobin thus making the bond substantially weaker than that of carbon monoxide and hemoglobin.

1.The two Beta globin chains aid the oxygen carrying ability of oxygen in red blood cells