Erythrocytes Essay

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1.Human Erythrocytes. Human erythrocytes have a life span of about 120 days in circulation. This life span is achieved even though they have no nuclei or internal repair mechanism and thus have no major biosynthetic repair mechanisms. Compared to other cells in the body for example neutrophils that have a life span of only 5 days (11) the human erythrocyte circulate through the body for a long period of time, a full circulation on average take about 20 seconds to complete (12). Its main function is to transport oxygen in hemoglobin to the tissues and surrounding organs. The cell can swell changing it osmotic pressure when oxygen or carbon dioxide is being transported, and can hold up too 150fL. (12) The human erythrocytes are formed through many components such as actin, spectrin and other protein that help the cell to form its shape and rigidity. Erythrocytes take up a large percentage of the overall cell population with 4-6 million of them per microliter.(12) The big issue is when the shape of the cell becomes mutated and the cell cannot carry out its normal biological process. With them being at such a high ratio in our body and their lack of a biosynthesis repair mechanism it can lead to disease’s to occur. 1.2 Mutations. 1.2.1 Sickle cell anemia. Human Erythrocytes can become misshaped due to mutations in its genetic structure. Sickle cell anemia is coursed by a single nucleotide mutation in the cells genetic structure. Specifically, in the beta chain of the hemoglobin protein, in the chain the valine is replaced with the glutamic acid. Given in the name of the disease the erythrocytes become sickle shaped and some stick together, causing blockages in values and capillaries around the body. Because of the deformed shape of... ... middle of paper ... ...dle of the spectrin tetramer. (10) The intrinsically unstructured protein β-spectrin C- terminal tail binds to the structured α-spectrin N-terminal tail. 1.9 Proteolysis. Proteolysis is the process by which a protease (enzyme) breaks down a protein into a polypeptide chain or amino acids. Proteolysis can break down proteins at a higher affinity when there in their primary structure. When proteins are folded and form a bundle the enzyme finds it difficult to attack the protein to break it down. This is why protein want to from the quaternary structure to make it less susceptible to this proteolysis attack. Stephanie A. Hill published a paper concluding: In spectrin, the alpha and beta chains are intrinsically unfolded proteins when they are not bound to one another. But when they bind together to form the tetramer in the “head to head” interaction they are fully
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