oxygen is given up by hemoglobin at the tissues. List 3 factors that promote this reduced...
How does Hemoglobin (Hb) bind oxygen with high affinity in the lungs, and then releases about a third of it in the tissues? How the affinity of hemoglobin to oxygen change when hemoglobin is in the lungs compared to when it is in the tissues? What factors influence the affinity of hemoglobin to oxygen and how?
What will happen if the levels of CO2 in the bloodstream increases? 1. Hemoglobin-oxygen affinity will go up 2. Hemoglobin-oxygen affinity will go down 3. Hemoglobin-oxygen affinity will be unchanged please briefly explain the answer
affinity of oxygen and hemoglobin and so 02 delivery to the tissues. affinity of oxygen to hemoglobin and so decreased 02 delivery to ti uestion 5 blood levels of CO2 can create which of the following effects on blood chemistry and breathing reflexes? Excessive H+ in blood results in acidosis which triggers increased breathing rates An increase in H+ ions leads to an increase in pH and thus alkalosis and an increase in breathing. HC03-ions lead to alkalosis of the...
Explain how pH, carbon dioxide, and 2,3-BPG promote the release of oxygen from hemoglobin. Why is it important to favor the release but not the binding of oxygen to hemoglobin?
In a mutant human hemoglobin, a mutation in the β chain abolishes binding of 2,3-bisphosphoglycerate (BPG) to the tetramer. How will this mutation influence the ability of this hemoglobin to give up oxygen at the peripheral tissues? Explain, briefly.
During aerobic activity, we depend on hemoglobin to pick up oxygen in the lungs and deliver it to tissues in a cooperative manner. Which of the traces on the graph shown accurately shows cooperative binding/release of oxygen from hemoglobin? 1.0 0.8 B 0.6 Y (fractional saturation) 0.4 0.2 0.0 0 50 200 100 150 pO2 (torr) Figure OA OB С
biochemistry
Question 2.(12 pts) O2 binding to Fe? in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the change in the shape of the heme that results in O2 binding. Page 4/7 b. How is the heme shape change communicated to the other subunits c. What is the role of Bisphosphoglycerate (BPG) in hemoglobin mediated oxygen transport? Question 3.(9 pts) You need to make up a 600 ml of a 40 mM solution...
2. What fraction of oxygen bound in the lungs is released in peripheral tissues for each hemoglobin? Which hemoglobin is better at transporting oxygen? Assume that the lung pO2 = 100 torr and that the peripheral tissue pO2 is 20 torr. Based on the shape of the saturation curve shown above, describe the effect of the Asp99Asn substitution on the cooperativity of oxygen binding? Is the cooperatively positively or negatively impacted by this mutation? 3. 4. In normal deoxyhemoglobin (hemoglobin...
O2 binding to Fe2+ in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the change in the shape of the heme that results in O2 binding. b. How is the heme shape change communicated to the other subunits c. What is the role of Bisphosphoglycerate (BPG) in hemoglobin mediated oxygen transport?
CIRCULATION: ANATOMY AND PHYSIOLOGY 1) Describe the composition (cells and/or proteins) of formed elements in the blood versus the plasma elements in blood. 2) Describe the features of an erythrocyte and how it helps promote the function of circulating gas through the body. 3) What is meant by cooperative binding? B) Hemoglobin shows cooperative binding. How does this help promote its function of gas delivery to tissues? 4) Identify at least two environmental conditions that can shift the affinity hemoglobin...