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Q: hemoglobin i:
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Q: Draw the structure of human blood carpusles?
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Q: What protein in a red blood cell carries oxygen?
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Q: 30. assicuatuib if 2alpha and 2 beta chains to form adult hemoglobin
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Q: PHOW does the oxygen binding curve of fetal hemoglobin differ from that of adult hemoglobin
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Q: What are the different parts of human blood? How does it tie into the concept of hemostasis?
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Q: Discuss what is the advantage of producing different hemoglobins at different stages ofdevelopment?
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Q: What is the main morphological difference between the RBC of frogs and humans?
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Q: Why is iron important to hemoglobin synthesis, and why is iron deficiency related to anemia?
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Q: What is the gene code for hemoglobin?
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Q: What is the composition of plasma membrane of human erythrocyte.
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Q: What are the six critical functions of blood
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Q: Why is it necessary to match the donor’s and the recipient’s blood before a transfusion is given?
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Q: How can the bloodcoagulation (clotting) processbe described?
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Q: Which characteristics of normal blood is difficult to be produced artificially?
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Q: Is red blood cells(erythrocytes) considered true cells histologically? Why or why not?
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Q: What molecular properties of red blood cells enable them to move through capillaries smaller than…
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Q: What do you mean by the term double circulation of blood in mammals?
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Q: Discuss why it is advantageous for humans to producedifferent hemoglobins at different stages…
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Q: Name cellular components of blood containing haemoglobin.
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Q: HOW Different Hemoglobins Are Expressed atDifferent Developmental Stages?
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Q: Why does the fish heart pump only deoxygenated blood?
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Q: What are the 3 main components of blood?
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Why is it necessary to separate oxygenated & deoxygenated blood in mammals & birds?
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- Myoglobin ... A. has higher affinity for O2 than hemoglobin does. B. consists of four polypeptide chains, just as hemoglobin does. C. has a lower affinity for O2 than hemoglobin does. D. is found in the interstitial fluids, in contrast to hemoglobin that is found in red blood cells. E. can bind four O2 molecules at once.Fetal hemoglobin binds 2,3 BPG with greater affinity than adult hemoglobin.TrueFalseWhich of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environments
- Which of the following statements is INCORRECT about how the components of hemoglobin are recycled? a. Iron ions are either stored in a phagocytic cell or circulate in the blood, bound to transferrin (a plasma protein). b. Each heme is stripped of its iron and converted to bilirubin, then excreted in bile. c. The alpha and beta chains are released into the bloodstream for use by other cells. d. Hemoglobin can be recycled only if phagocytized by macrophages.BIOCHEMISTRY Using relevant stoichiometric equations provide a detailed description about mechanisms of hemoglobin autoxidation don't copyWhat is the molecular basis for the difference in the electrophorentic pattern between normal hemoglobin A and hemoglobin S?
- Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
- The PO2 of placental blood is about 40 mmHg. What are the O2 saturations of maternal and fetal hemoglobin at this PO2?Scenario: In Charles’ blood, the partial pressure of CO in the blood (0.4 mm Hg) is far lower than the partial pressure of O2, yet the percent saturation of hemoglobin by each gas is approximately equal. What does this tell you about the affinity of hemoglobin for CO?In humans, iron is a trace element required for the proper functioning of hemoglobin, the molecule that carries oxygen in red blood cells. What might be the effects of an iron deficiency?