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Rose Sciendez Case Summary

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Assignment 1
1) When verified the blood samples, a normal sample of blood was bright red in colour, however, Miriam’s blood colour was much duller red in comparison to the normal sample. Under the microscopic view, for normal blood cells, it was observed that the cells were spherical and completely enclosed. However, this was not the case in Miriam’s blood cells. In her microscopic view, few of her cells were not spherical, they were straight instead. Therefore, yes, Miriam red blood cells do show phenotypic characteristics of sickle-cell disease as her cells do appear in sickle shape. About 33% of her cells show that she has been affected by Sickle-cell anemia (number of sickle shaped cells divided by total number of cells in the microscopic …show more content…

The migration pattern of the patient did show mutation in the protein. The patients RBC count is also quite high. Rose appeared to be heterozygous as only her father suffered from the abnormal complexion, but her mother and sister had normal complexions. When Rose’s peptide sequence was observed, on the 99th position, Asp- was replaced by His- amino acid. A change in the beta chain’s 99th amino acid results in replacing His- amino acid instead of Asp- amino acid, which is why abnormality in the haemoglobin is caused (Jones et al. 1967). A study was done in order to show the increase in oxygen affinity due to hemoglobin Yakima (Jones et al. 1967). The increase in oxygen affinity by the haemoglobin Yakima and few other similar abnormal haemoglobins might have been due to similar structures and might explain possible characteristics of reversible combinations with oxygen present in the normal haemoglobin (Jones et al. 1967). They study also concludes that the change in beta chain resulted due to slow electrophoretic mobility in the haemoglobin Yakima (Jones et al. 1967). The study provided an explanation that on the beta carbon with the alpha NH group, the hydrogen bond between OH and COO- group is present of the 4th position in the helix (Jones et al. 1967). However, this intrahelical bond is not formed by histidine amino acid at the position G1 in haemoglobin Yakima (Jones et al. 1967). This means, if an intrahelical hydrogen bond forms between alpha carbon of FG 5 and alpha NH group at G4, the size of the G helix would vary (Jones et al.

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