True or false PFC's (perfluorinated hydorcarbon chains) can supply oxygen but do not dissolve well in blood plasma.  In order to use PCF's as a blood substitute patients must breathe 70-100% oxygen through a mask.  PFC's are eventually removed by the body through exhalation.

In a study of O2 uptake by muscle at high altitude, a physiologist prepares an atmosphere consisting of 79 mole % N2, 17 mole % 16O2, and 4.0 mole % 18O2. (The isotope 18O will be measured to determine O2 uptake.) The total pressure is 0.75 atm to simulate high altitude. Calculate the mole fraction and partial pressure of 18O2 in the mixture.

Following several days at high altitude the body responds to the decreased oxygen content of the atmosphere by increasing the amount of 2,3-bisphosphoglycerate it produces. Based on this information and refering to the graph below, identify the correct response from the options. Y (fraction saturation) 1.0 0.8 0.6 0.4 0.2 0.0 0 20 Oxygen Binding plot 40 60 p02 (torr) 80 100 A) Curve y=high altitude and gives a greater release of oxygen to the tissues B) Curve x = high altitude and gives a greater release of oxygen to the tissues C) Curve y=high altitude and allows more oxygen to be bound at low oxygen levels D) Curve x = high altitude and allows more oxygen to be bound at low levels

Exposure to air containing 600 ppm CO for 30 minutes results In an actual HbCO blood concentration of 10%. Estimate the percentage of the equilibrium saturation value of HbCO.

To demonstrate an understanding of oxyhemoglobin binding, insert a word from the list in each blank to complete the statements. Not all terms will be used. increased A right shift of the oxy-hemoglobin curve signifies a affinity for oxygen. hold acidic A temperature will cause a right shift of the oxy- hemoglobin curve. basic A more pH than normal blood pH will cause a right shift higher of the oxy-hemoglobin curve. As a person exercises, their muscles give off heat which raises the temperature of the blood. This will cause hemoglobin to more oxygen at the cells. lower release decreased

Crocodiles can use virtually 100% of the oxygen in its blood, whereas humans can extract only about 65% of the oxygen in their blood. Crocodile hemoglobin (Hb) binds HCO3, rather than 2,3-bisphosphoglycerate (BPG), when in the T-state. Which of the following best explains why HCO3¯ in the crocodile works better than 2,3-BPG in humans to help the Hb to release more of its bound oxygen? Crocodile Hb binds more oxygen than human Hb, and so the crocodile has more oxygen available than humans do. The [HCO3] varies with the amount of oxygen used, whereas the [BPG] in human erythrocytes is constant regardless of need. Humans require their hemoglobin to be sensitive to [BPG] in order for HbF (fetal Hb) to have a higher affinity for oxygen than maternal Hb. Since crocodile Hb binds HCO3, the HCO3 will not be available to bind to H+ (Bohr protons), and so more oxygen will be released to the tissues. Crocodiles are cold-blooded and so do not need as much oxygen as humans; this is why they can…

True or false Chemically-linked hemoglobin moelcules can stay in the blood for as long as 72 hrs. Cow hemoglobin can be safelty used by humans.  Free hemoglobin produces vasoconstruction of blood vesselsand increases blood pressure in patients.

Below is the reaction catalyzed by carbonic anhydrase. Please answer the following questions. CO₂ + H₂O → H+ + HCO3* a. The forward reaction is favored in the lungs b. When protons decrease the pH [Select] [Select] c. CO₂ acts directly as a [Select] hemoglobin by reacting to form carbonic Answer 1: lungs Answer 2: decreases Answer 3: HbR Answer 4: negative heterotrophic state is favored Answer 5: and the allosteric effector of reacting to generate protons another allosteric effector that stabilizes the T state

Lowering the pH from 7.4 to 6.8, which can occur during heavy respiration, reduces the Hill coefficient for oxygen binding to hemoglobin.    True or False

Below are multiple oxygen binding affinity curves for hemoglobin. The affinity curve for normal hemoglobin in blood is represented by curve "D," at a pH of 7.2 and at a concentration of 5mM BPG and 26 mM CO2. O₂ saturation (%) 100 Answer 1: B Answer 2: [Select] Answer 3: B Answer 4: 80 A 60 1. How would changes to acidity, BPG concentration and CO₂ levels affect the binding affinity curve and p50? lower than Answer 5: E 40 1. BPG concentration is decreased to 3mM: The binding affinity curve would look like B. The p50 would be lower than normal (D). 2. pH is increased to 7.6: The binding affinity curve would look like B. The p50 would be [Select] normal (D). 20 3. CO₂ concentration is increased to 30 mM: The binding affinity curve would look like. [Select] The p50 would be Answer 6: 0 normal (D). II. The hemoglobin has been treated with a denaturing solution which disrupts quaternary structure only, and has a binding affinity resembling myoglobin. The binding affinity curve would look…