Transport of gas Coursework Example | Topics and Well Written Essays - 500 words

Transport of gas - Coursework Example 89). This further buttresses the high affinity for oxygen of the fetal hemoglobin. Additionally, fetal hemoglobin lacks the interaction with 2,3-BPG. Due to a change on a single amino acid on the binding pocket of 2,3-BPG, it binds less to fetal hemoglobin (Hall, 2010, p.58). This phenomenon explains the high affinity of fetal hemoglobin for oxygen as compared to maternal adult hemoglobin. c) After birth, the fetal hemoglobin is replaced with adult hemoglobin. Therefore, the oxygen-dissociation curve shifts to the right. It confers advantage to the infant after birth because the adult hemoglobin readily gives out oxygen to the tissues as compared to fetal hemoglobin, despite the fact that fetal hemoglobin has a higher affinity for oxygen. It would prevent tissue ischemia (Maryland Department of Health and Mental Hygiene, 2013) b) An increase in the partial pressures of carbon dioxide will shift the curve to the right. Carbon dioxide reduces intracellular pH as a result of the formation of bicarbonate ion. Formation of bicarbonate releases a proton into plasma, therefore reducing pH which has an effect of shifting the curve to the right (Ganong, 2005, p. 90). Similarly, pH affects the oxygen-dissociation curve. A decrease in pH shifts the curve to the right. At molecular level, a high H+ concentration, some amino acids such as Histidine 164 exist in their protonated form predominantly. They; therefore, form ion pairs which maintains deoxyhaemoglobin in the T state. The T state of hemoglobin has a lower affinity for oxygen; therefore, with increased acidity levels, hemoglobin binds less oxygen. This phenomenon is known as the Bohr Effect(Hall, 2010, p.57).. Maryland Department of Health and Mental Hygiene. Fetal Hemoglobin (Hemoglobin F) Fact Sheet. Available from from Maryland Department of Health and Mental Hygiene: http://phpa.dhmh.maryland.gov/genetics/SitePages/hemo_f.aspx [Accessed: