Lab Report On The Concentration Of Haemoglobin

“Erythrocytes contain haemoglobin, an important respiratory pigment that is essential for human life” (Strech, Beryl; Whitehouse, Mary;, 2010) Haemoglobin is very important because it is an iron-containing protein.

The structure and colour of a red blood cell is come from the haemoglobin which consists of four folded chains of amino acids, this forms the sub groups which are smaller haem groups that are attached together. For each haem group there is an iron molecules which is in a ferrous state (Fe2+), there is 2 sub unit of Alpha (α) which consists of 141 amino acid and 2 sub unit of Beta (β) which consists of 146 amino acid. The haem group keeps the structure of the haemoglobin in place. When an oxygen (O2+) molecule is carried by the red blood cell, it forms a weak ionic bond with the Fe2+ molecule in the four haem group, this is then transported to the rest of the body. Haemoglobin and oxygen combine to form oxyhaemoglobin, this is the reason the blood cell is bright red, when the oxygen is transported to the region it is needed the blood turns back in to haemoglobin this is where its deoxygenated blood and it returns back to the heart then to the lungs where diffusion occurs (CO2) removed through the capillary wall and O2 is absorbed into the blood). Blood being unable to pick up 02 molecules would mean less oxygen will be able to be transported, which would mean that the heart would have to work much harder to transport the small amount of oxygen in the body, this

The blood protein in Methemoglobinemia are unable to carry oxygen, which makes it harder for the tissue to get the amount of oxygen

Methemoglobinemia can be either acquired or congenital. When methemoglobinemia is acquired the mechanism that reduces methemoglobin is not able to keep up with the amount of oxidation that is occurring due to the various methods of acquiring methemoglobinemia [2]. There are two primary reasons for congenital methemoglobinemia; either there is a presence of an abnormal structure of the hemoglobin molecule, called hemoglobin M, or a deficiency in the enzymes cytochrome b5 methemoglobin reductase or glucose-6-phosphate dehydrogenase (G6PD) [5]. There are two main types of congenital methemoglobinemia, type I and type II. Type I methemoglobinemia is where the enzyme deficiency only affects the erythrocytes, and is easily

1.Full blood counts: To assess the Hb for evidence of anemia, WBC for evidence of infection.

A hemoglobin test is normally part of the CBC and is used to measure the amount of hemoglobin in the blood. Hemoglobin is the protein carried by the red blood cells that transports oxygen to the body's tissues and also carries away carbon dioxide from the tissues to the lungs. If a hemoglobin test results in a low hemoglobin count, it's usually a sign of anemia

Under normal circumstances RBCs are flexible oval biconcave disks and move easily through capillaries carrying oxygen to all parts of the body. The presence of polymerized HbS in the blood stream cause RBCs to be stiffer, fragile, rigid, and induce sickling of the RBCs (21).

In 1747 Dr Vincezo Menghini wrote he had blunt blood to obtain a red powder substance and discover this substance was attracted to magnets, quickly confirming that this substance contained iron. Friedrich Ludwig Hunefeld many years later confirm these findings and chemically split the blood pigments into two components. A protein structure known as globulin and a red compound with iron oxide known as haem. This was the beginning of iron therapy for anaemia. It was Hopp Seyler that called the term haemoglobin in 1862 and determine its structure for further studies. In this research paper, it will discuss the importance roles haemoglobin play in the physical structure. It will explore the importance of gas exchange how carbon dioxide enters and exit from the body during breathing and their structure and function.

When the alpha chains are deleted, the iron that is supposed to attach to the alpha chains which contain a heme molecule becomes free iron. This is because the iron has nowhere to attach if its chain is missing. This free iron can be dangerous to the body because of its toxic nature. If the heme molecules are not binding, iron cannot be stored there and therefore be transported to the red blood cells. This means that oxygen is not being transported to the hemoglobin protein. The hemoglobin protein has to be released from the red blood cells and be released into the plasma by enzymes that contain heme. After the enzyme release the protein, the red blood is destroyed and hemoglobin can release oxygen into the bloodstream. With Alpha Thalassemia, the low functioning numbers of hemoglobin are not enough to provide stable oxygen levels. If the levels are too low anemia is developed and blood transfusions are given to provide health red blood cells and hemoglobin proteins that can have alpha chains. The influx of new hemoglobin proteins allows for iron to have heme molecules that are in the alpha chains to bind. This allows for hemoglobin proteins to increase and numbers allowing oxygen to be successfully released into the blood stream. However, that still leaves the free iron that did not have a heme molecule and alpha chain to attach to. This leads to high levels of iron that were once low before the new hemoglobin proteins were delivered because the bodies cannot produce

- The developing fetus does not breath by drawing in air into its lungs like an adult does. Instead, the fetus draws its oxygen from the mother’s blood where the oxygen content is low. The hemoglobin in adults consist of two alpha and two beta subunits. Fetal hemoglobin consists of two alpha and two gamma subunits. This allows hemoglobin to bind oxygen with higher affinity compared to adult hemoglobin, allowing the extraction of oxygen from maternal circulation. It Is important in fetal development because fetal hemoglobin is the main oxygen transport protein during the last stages of development.

Hemoglobin is present in red blood cells and carries oxygen from the lungs to tissues and returns carbon dioxide from tissues back to the lungs. Met Hemoglobin is a form of the oxygen-carrying part of Hemoglobin of which a small amount is present in human blood and produced automatically. However, if produced in large amounts it can cause coma and even death. Increased levels of Methaemoglobin can be caused by the ingestion of chemicals such as Cyanide and can be detected in blood stains at a scene of a crime as enhanced levels of Met Hemoglobin changes blood upon leaving the body from red to a dark brown in

HDN always leads to anemia or low blood count, because of the prolonged destruction of the red blood cells. Erythroblasts (known as immature red blood cells) will also present in the baby’s circulation. After the baby is born, he or she may have a pale skin due to the

The second crucial function of hemoglobin according to Keohane et al. (2016) together with McPherson & Pincus (2017) is the transport of carbon dioxide (Figure 9). They stated that: “In venous blood, the carbon dioxide diffuses into the red blood cells and combines with water to form carbonic acid (H2CO3). This reaction is facilitated by the RBC enzyme carbonic anhydrase. Carbonic acid then dissociates to release H+ and bicarbonate (HCO3-).

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),

The haemoglobinopathy, SCD is a severe blood disorder that is accountable for 33.5% per 100,000 hospital admissions in the UK (Aljuburi et al, 2012). The number of admissions has seen a steady increase over the last few years. In 1910, James Herrick was first to record that a Bajan male suffered from anaemia due to sickled red blood cells however in 1949 Linus Pauling identified that there was a molecular difference in the haemoglobin of a sickled and wild-type individual (Gabriel, A. and Przybylski, J., 2010). Ingram V. made the further observation that a single nucleotide polymorphism (SNP) resulting in valine instead of glutamic acid led to the conformational change in haemoglobin (Gabriel, A. and Przybylski, J., 2010).