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Essay / Research Paper Abstract
A 4 page review of the biochemical basis of sickle cell anemia. The author discusses the pathophysiology of sickle cell anemia from a cellular perspective rather than a sociological perspective. Bibliography lists 7 sources.
Page Count:
4 pages (~225 words per page)
File: AM2_PPsickC3.rtf
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Unformatted sample text from the term paper:
The pathophysiology of Sickle Cell Anemia is determined at a biochemical level. The disease is one of
the most common forms of thalassaemia, a family of genetically carried disorders which affect the bodys ability to synthesize haemoglobin. Sickle Cell Anemia is the result of an individual
receiving two genetic copies of a genetic mutation which evolved in response to the parasite-born disease malaria. The U.S. Department of
Energy (2005) reports that the sickle cell mutation occurs on the HBB gene found at "in region 15.5 on the short (p) arm of human chromosome 11". The mutation
occurs on Locus: 11p15.5 (U.S. Department of Energy, 2005). The HBB protein is reported to be 146 amino acids long and to have a molecular weight of 15,867 Da
(U.S. Department of Energy, 2005). The formation of Howell-Jolly bodies is a reflection of the disease and one of the biochemical characteristics that is useful in diagnosis (Carley,
2005). In a normal individual hemoglobin A, that component of the red blood cells which carries oxygen throughout the body, is
spherical and soft and as such is ideally suited to traverse the sometimes constrictive environment of the small blood vessels (Norris, 2004). Normal hemoglobin is responsible for the transport
of oxygen from the lungs to the various tissues of the body (Zimmermann et. al., 2005). Hemoglobin is a complex protein. Each individual molecule of hemoglobin is comprised
of five percent heme, this is complemented by ninety-five percent globin (Hickman Hickman and Hickman, 1974). It is the heme which
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