Human Physiology: From Cells to Systems (MindTap Course List)
9th Edition
ISBN: 9781285866932
Author: Lauralee Sherwood
Publisher: Cengage Learning
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- Select all answers that applyarrow_forwardWhich of these occur when hemoglobin releases oxygen? Select all that apply. O Conformation is shifted toward the T-state BPG can bind in the central channel O Fe2+ is at the center of a planar heme grouparrow_forwardIn 1913, Archibald Hill described an alternative formulation for cooperative processes such as the binding of oxygen by hemoglobin by considering the hypothetical equilibrium Hb+ n0₂ Hb(0₂)n 2 Analysis leads to the Hill equation: n p02₂" ( Y log (₁ x x ) = log Y (^_^) log where Y is the fractional saturation. This equation suggests that a plot of log with slope n. Plots for myoglobin and hemoglobin are shown here: 3 2 1 O -1 -2 -3 P50 + n = nlog (pO,) – n log(P5o) Myoglobin (0.25, -0.25) -1 0 1 2 log (pO₂) (3.0, 2.5) 3 4 (^_^) log 3 2 1 O -1 -2 -3 -4 (0, -3.4) -1 0 Y Y versus log (pO₂) should yield a line Hemoglobin (2.1, 2.5) - (0.7, -2.0) (1.9, 1.3) (0.4, -3.5) 1 2 log (pO₂) - (2.4, 2.4) 3 4arrow_forward
- Which of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at differentarrow_forwardWhich five statements about hemoglobin and myoglobin structure are true? Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to Fe²+ in heme. Heme is composed of an organic protoporphyrin component and a metal atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron atom. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom.arrow_forwardWhich of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.arrow_forward
- Which of the following statements regarding the transport of oxygen by hemoglobin is correct? Upon binding of oxygen to heme, a shift in the position of the distal His ultimately induces the switch from T to R states When fully bound to oxygen, AG(R-state)arrow_forwardSelect all answers that aarrow_forwardThe graph below shows the O₂-binding curves for myoglobin (Mb) and hemoglobin (Hb). a. 100 80 60 40 20 0 0 20 40 60 80 100 pO₂ (torr) a. Use the graph to determine the Kd of myoglobin for O₂ (show your approach). Write that in the provided space. b. What is the difference between myoglobin and hemoglobin that cause the O₂- binding curves to so be different? Answer in the provided space. c. Why is it important that hemoglobin has these particular O₂-binding characteristics? Answer in the provided space. YO₂arrow_forwardContrast the characteristics and function of myoglobin versus hemoglobin 1.which is impacted by pH and temperature?arrow_forwardWhich of the following statements does NOT apply to the K value in the equation for the oxygen binding curve of myoglobin? It is numerically equal to p50. O A. It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied. В. If Y> K, then myoglobin is less than 50% saturated with oxygen. OC. O D. It is a measure of the affinity of myoglobin for oxygen. OE. It is the value of po2 at which Y = 0.5.arrow_forwardWhich statement about BPG's interaction with hemoglobin is correct? Group of answer choices BPG binds with a stoichiometry of one molecule per hemoglobin subunit Without BPG, hemoglobin would not be able to release oxygen in muscle tissue BPG stimulates the ability of hemoglobin to take up oxygen in the lungs BPG binding counters the Bohr effect in muscle tissue, causing an increase in pH BPG's negative charge interferes with ion pair formation, thus favoring the R statearrow_forwardarrow_back_iosSEE MORE QUESTIONSarrow_forward_ios
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