a. How many subunits does hemoglobin have? What are their conventional names? b. Identify the oxygen binding sites on hemoglobin. How many oxygens can one molecule of hemoglobin bind? How many oxygens can one subunit of hemoglobin bind? c. Identify the central cavity of hemoglobin. Is it the same or different than the oxygen binding site of hemoglobin?

x The Bohr effect describes the impact of changes in serum pH and CO2 concentrations on the oxygen dissociation curve of hemoglobin. This effect is physiologically important because it allows the body to adapt to changing conditions and provide enough oxygen to different types of tissues. **Plot the curves of hemoglobin oxygen saturation for patients in conditions of acidosis (serum pH below 7.34) and alkalosis (serum pH higher than 7.45) and compare it to the one in normal conditions. ** **When tissues, such as muscle tissue, are performing large amounts of strenuous activity the increase in metabolic activity produces CO2 as waste. Once in the bloodstream the enzyme carbonic anhydrase speeds up the conversion of CO2 to bicarbonate and protons. How does this affect the release of oxygen to the tissues?** **2,3-bisphosphoglycerate is an allosteric inhibitor of oxygen binding to hemoglobin. Acclimatization to high altitude involves numerous physiological and biochemical changes,…

What other diseases are associated with estraneous forms of hemoglobin subunits in the human adult?

From your graph, estimate the P50 for normal hemoglobin and the mutant corresponding to your student number and explain if these results support your expectations regarding the mutant's oxygen affinity compared to normal hemoglobin. ف C Normal Yakima pO2 (torr) Yo2 Yo2 10 0.05 0.10 15 0.10 0.25 20 0.25 0.45 25 0.50 0.70 30 0.75 0.85 40 0.85 0.95 60 0.95 0.98 H