Hemoglobin Synthesis Lab Report

Sickle Cell Disease is an autosomal recessive genetic disease that occurs due to a mutation in the β-globin gene of hemoglobin. Autosomal meaning that it is not linked to a sex chromosome, so either parent can pass on the gene to their child. This mutation is a result of a single substitution of amino acids, Glutamic for Valine at position 6 of a β globin chain. The presence of this mutation causes

The effects of the sickle cell mutation can be traced back to DNA in which the mutated gene is replicated and transcribed to mRNA. This mRNA is then used to synthesize polypeptides in the ribosomes where it translates the mutant genetic code (GUG) which codes for valine. Instead of the genetic code for glutamic acid (GAG) which is the amino acid found in the normal haemoglobin. This causes the haemoglobin to be clumped up together in the red blood cells and depriving them if oxygen causing a sickle shaped cell instead of the normal round, biconcave

Sickle cell anaemia is a disorder affecting the red blood cells and up to 100,000 people are estimated to have the disease in the USA (Centre for Disease Control). Due to a genetic mutation in the gene responsible for the production of haemoglobin (MayoClinic, 2014) the red blood cells, which are usually a biconcave disk in shape, become sickle (bent) shaped (Figure 1) and the haemoglobin that the red blood cells contain is defective. Haemoglobin is a protein that carries oxygen (which has bind to the haemoglobin) around the body from the lungs after gas exchange. Having defective haemoglobin, as is the case with sickle cell anaemia, means

In the three experiments that we did we extracted dan from strawberries, E.coli, and wheat germ. In each of the experiments we had to open the nuclear envelope in some way with the strawberries we did this by freezing them so that the expanding water would break the nuclear envelope and allow the dan to be extracted. We also smashed them up to help facilitate in the breaking up of the cells. In the wheat germ we used a mortar and pestle to grind the wheat into a fine powder to release the dna.

Normal hemoglobin is more flat shaped while a sickle cell takes on a curved shape because the red blood cells are destroyed by the disease (Sickle cell anemia, 2014). The sickling continues to occur leaving the damage to the red blood cells irreversible. The cells new shape causes them to become less functional and more rigid which can lead to blockage of the blood vessels. This disease causes many vascular complications because of this blockage (Steinberg, 2014).

The tertiary structure of hemoglobin is different for the two types of polypeptides present, each getting their shape due to bonding interactions among the amino acid R groups, which are in different orientations in alpha and beta folding. The tertiary structure has the hydrophobic amino acids in the interior and the hydrophilic amino acids bound outwards so dipole-dipole interactions can occur. As a result of the tertiary structure the three dimensional structure for each of the globular proteins is determined and they are now able to form a quaternary structure with each other. In the quaternary structure the four polypeptides are bound together by strong hydrophobic interactions, and the alpha chains and beta pleated chains are bound together by ionic and hydrogen bonds

Sickle-cell disease majorly affects the hemoglobin that is present in our blood. The job of hemoglobin is to help transport oxygen and carbon dioxide to and from the cells throughout our body. Hemoglobin is present specifically in our red blood cells. Each red blood cell contains two hundred and eighty million hemoglobin molecules. Red blood cells normal shape is a biconcave shape because of the lack of many organelles and a nucleus. The shape is so important to a red blood cells functioning that if it is not shaped normally it has major consequences. The shape helps them to fit through capillaries easier and also allows for an increased surface area which results in easier gas exchange. Sickle-cell disease is a genetic disease that causes issues in the oxygen/carbon dioxide carrying hemoglobin molecules that are present in our red blood cells.

Sickle cell disease affects approximately 100,000 Americans and millions across the globe (Sobota, 2015). The three most common types of sickle cell disease are Hb SS (sickle cell anemia), Hb SC, and Hb S beta thalassemia, with Hb SS being the most common type (Harris, 2001). Sickle cell disease occurs in individuals who inherit the mutated hemoglobin gene, from one or both of their parents. The mutated hemoglobin, known as Hb S, crystalizes and join together “into many small cords, which form chains that look like twisted wires” (Harris, 2001, p. 20). Stretched to contain the Hb S crystals, the red blood cells take on spike and sickle shapes; this is how the name for the disease came about (Harris, 2001). Deformed, the sickled cells have a hard time moving through the blood stream and can eventually pile up in the blood vessels, having life-threatening consequences. Although oxygen can reverse the sickling process in cells, turning Hb S back into a liquid, after a few sicklings the red blood cells’ membrane is permanently damaged and the cell will remain sickled.

Sickle cell anemia (SCA) is one of the most prevalent recessive autosomal diseases in the world, affecting approximately 300,000 newborns each year, with the number predicted to rise to 400,000 by the year 2050. It is a disease of the β-globin gene (HBB), whereby a single nucleotide polymorphism (SNP) causes the β6 glutamic acid (Glu) to mutate into valine (Val). The resulting Glu6Val changes the conformation of the red blood cell (RBC) because Val is hydrophobic and Glu is acidic, polar, and has a negative charge. This SNP causes the hemoglobin (Hb) to alter its tertiary structure, forming Hb S which then creates long polymers that alter the RBC’s shape. Many forms of treatment for SCA are being researched, with some of the most promising results coming from gene therapy. Although gene therapy does provide a promising outlook for many diseases, the technique is still under

Essentially, there is an incorrect base- pair change when the Deoxyribonucleic Acid strand are being duplicated, exchanging the “the sixth amino acid from glutamic acid to valine causing the mutated hemoglobin (HbS) to polymerize” or change the shape of each cell (Adams1). The most severe form of Sickle Cell Disease is Hemoglobin SS, in which both parents are carriers of Sickle Cell gene, “SS”, and ultimately reproduce a child that has SCD. In Hemoglobin SC, one parent has the gene “S” while the other has the trait “C”, thus having a milder form of Sickle Cell Disease (Stuart7). Sickle Cell Anemia or Hemoglobin S beta thalassemia is another form of SCD, where one parent has the “S” gene while the other parent has an additional form of anemia or thalassemia (CDC5). Due to the constricting shape of the erythrocytes, the blood cells began to die at an alarming rate causing the body to be deprived of oxygen, creating a number of other health complications. Stroke, neurocognitive functions, infections and the increased risk of death can occur if left untreated. Amongst individuals with SCD, the risk of having a stroke is increased, especially in children (Adams1). Stroke is said to be caused by the constriction of blood vessels and lack of oxygen in the brain that is associated with Sickle Cell Disease. However, because of the stroke increase in

Sickle cell disorders are a group of inherited disorders where adult haemoglobin (HbA) is replaced by sickle haemoglobin (HbS) due to the substitution of glutamic acid by valine at the position 6 of the beta globin chains3. In addition, these disorders can be of various conditions, however, we will mostly on the two most known conditions which are sickle cell anaemia (HbSS) and sickle cell trait (HbAS). The other conditions are those where sickle cell disorders is associated with other disorders such as beta thalassaemia or haemoglobin C (HbSC). Sickle cell anaemia refers to the form of sickle cell disorders where the patient receives a copy of the mutated gene from each of his parents (homozygosity) whereas in sickle cell trait, the individual only gets one copy of the mutated gene from one his parents

Sickle cell anaemia (SCA) is a class of transformation disorder in the β globin gene, which leads to the development of insoluble, sickle shaped red blood cells (RBC). The red blood cell (RBC) consists of two α globin chains and two β globin chains, forming the oxygen carrying molecule haemoglobin. Upon being oxygenated, the three-dimensional structure of sickle RBC is said to be normal but abnormal when it becomes deoxygenated. This is because the β sickle globin polymerised more than normal β globin during deoxygenating process. Thus RBC tends to shape itself into a crescent resulting in the slowness of the blood flow, which can cause the organs to be damaged, vaso-occlusive crises and stroke. Sickle RBC have a short lifespan than normal

The hyphotesis created for this experiement was accurate. Each element received a different reaction for each of the tests. No test had a similar outcome for both Iron or Sulfur. The reaction always proved to be quite different and even the oposite. Iron reacted to magnet, mixed with the substances while Sulfur did not react with the magnet nor did it mix with either water or M Hydrochloric Acid. This experient however could have had a couple of mistakes. The measurments werent exact ones. It would be impossible to do so everytime and the amount of substance or elements would always be a little off.

Hemoglobin is present in red blood cells of the body and transport oxygen from lungs to the rest of the human body (National, 2015). Humans carry different types of hemoglobin, but there are three common types found in the gel electrophoresis. One of the test blood that help people to diagnose any disease is the hemoglobin electrophoresis. Hemoglobin electrophoresis test looks at the different types of hemoglobin in the blood, and can help diagnose the type of anemia that the person could have (National, 2014). The three common types of hemoglobin presents in humans are normal hemoglobin, sickle trait hemoglobin, and sickle cell hemoglobin. Abnormal hemoglobin, called hemoglobin S, causes sickle cell disease (SCD). The sickle cell hemoglobin

Investigating haemoglobin (Hb) concentration in blood samples using the haemoglobincyanide method and in foetal haemoglobin samples