Determine the Hill coefficient, n, for myoglobin (Mb), hemoglobin (Hb), and recombinant hemoglobin (HbX). Given the results of the Hill plot and the dissociation curves, which of the following are true?Oxygen binding by HbX is less cooperative than for HbThe Hill coefficient for Hb is equal to the number of hemoglobin O2 binding sitesOxygen binding by Hb is less cooperative than for Mb.HbX will load less O2 in the lungs and unload less O2 in active tissues than normal Hb. A Hill plot uses the Hill equation to quantitatively assess thedegree of cooperativity in binding. The fractional saturation (Y) of hemoglobin by O, can be expressed as a function ofThe researcher uses the oxygen dissociation curve data in aHill plot, plotting log () versus log pO,.Hill plothemoglobin's Ps0 -2.00-pO2+ P50 "1.50Yo,1.000.50Myoglobin0.00The fractional binding equation for hemoglobin can0.25 0.50 0.75 1.00 1.25 1.50 1.75 2.00-0.50rearranged.8 -1.00-MutatedpO, "P50 "Y-1.50- hemoglobinHemoglobin1- Y-2.00--2.50Taking the log of both sides yields the Hill equation, with the-3.00log(pO,)value of n equal to the Hill coefficient.Determine the Hill coefficient, n, for myoglobin (Mb),()-Yhemoglobin (Hb), and recombinant hemoglobin (HbX).log1 - Yn log (pO,) – log P50 "Mb Hill coefficient =Hb Hill coefficient =Given the results of the Hill plot and the dissociationHbX Hill coefficient =curves, which of the following are true?Oxygen binding by HbX is less cooperative thanfor Hb.The Hill coefficient for Hb is equal to the number ofhemoglobin O, binding sites.Oxygen binding by Hb is less cooperative thanfor Mb.HbX will load less O, in the lungs and unload lessO, in active tissues than normal Hb.

Oxygen dissolves pretty well in water and more oxygen curves by binding it to carrier molecules.…

Given the results of the Hill plot and the dissociation curves, which of the following are true? Oxygen binding by HbX is less cooperative than for Hb The Hill coefficient for Hb is equal to the number of hemoglobin O2 binding sites Oxygen binding by Hb is less cooperative than for Mb. HbX will load less O2 in the lungs and unload less O2 in active tissues than normal Hb

Given the results of the Hill plot and the dissociation curves, which of the following are true? Oxygen binding by HbX is less cooperative than for Hb The Hill coefficient for Hb is equal to the number of hemoglobin O2 binding sites Oxygen binding by Hb is less cooperative than for Mb. HbX will load less O2 in the lungs and unload less O2 in active tissues than normal Hb

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohr effect from the molecular perspective. Be sure to include discussion of what causes this (i.e. specific amino acids), why the curves are right shifted with decreasing pH, and why this is logical in delivery of 02 to areas of higher demand. 100 Myoglobin 80- pH 7.6 60 pH 7.4 pll 7.2 40- pH 7.0 pH 6.8 20- Venous 0- 0. 20 10 60 80 Percent saturation
A new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?
calculate the actual free energy of hydrolysis of ATP, delta Gp in the erythrocytes of a new species. The standard free-energy of hydrolysis of ATP is also -30.5kJ/mol in this species, but the concentrations in this specie's erythrocytes are 0.00775 mM ATP, 0.00027 mM ADP and 0.00418 mM Pi. Assume the pH is 7.0 and the body temperature of this species is 43.0oC. Calculate your answer as kJ/mol to two decimal places.
pO2 in tissues p02 in lungs 1.00 Oxygen-binding curves for normal Normal Hb hemoglobin, 50% carboxyhemoglobin, and hemoglobin from 0.8 an anemic individual. 0.6 Y 50% COHB 0.4- Anemic individual 0.2 4 8 12 pO2 (kPa) Box 5-1 Figure 2 Lehninger Principles of Biochemistry, Seventh Edition O 2017 W. H. Freeman and Company r aye i UIE I. Answer the following questions. Do not forget the units. 1) From the binding curve for normal Hb shown above, what is the Ka of normal hemoglobin?
Calculate the fractional saturation for emperor penguin myoglobin, which has a p50 value of 2.5 torr, at 30 torr. Express your answer with 2 digits to the right of the decimal point. fractional saturation = (Tolerance is +/-2%) eTextbook and Media
Calculate the hemoglobin concentration of an unknown sample given the following info: concentration of known = 12.5 g/dl; absorbance of unknown = 0.48; absorbance of known = 0.65 a. 16.9 g/dl b. 9.2 g/dl c. 8.7 g/dl d. 11.3 g/dl e. 10.4 g/dl
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Measurements of oxygen binding by whok human blood, at 37 °C, at pH 7.4, and in the presence of 40 mm Hg of CO, and normal physiological lkvels of 2,3-BPG (5 mmol/L of cells), give the following: Po, (mm Hg) % Saturation (=100 x Yo) 10.6 10 19.5 30 27.4 50 37.5 70 50.4 85 77.3 96 92.3 98 (a) From these data, construct a binding curve, and estimate the percent oxygen saturation of blood at (1) 100 mm Hg, the approximate partial pressure of O, in the lungs, and (2) 30 mm Hg, the approximate partial pressure of Oz in venous blood. (b) Under these conditions, what percentage of the oxygen bound in the lungs is delivered to the tissues? (c) Using the data in Figure 7.27, repeat the calculation of part (b) if the pH drops to 6.8 in capillaries but goes back to 7.4 as CO, is unloaded in the lungs.
The erythrocyte sedimentation rate (heaviness) test of a blood sample is often used as a diagnosis of immune disorders and some other diseases. Assuming that the red blood cells are about a sphere with a diameter of (approximately 5 um) and a density (g/ml 1.125), and the density and viscosity of the plasma in which the red blood cells are settled (Pa.s), (1025 kg/m3 10-3 x 1.5) On arrangement and acceleration m/s2 9.81 Calculate the erythrocyte sedimentation rate (settlement rate).
Which of the following is correct concerning the oxygenation plot of proteins X and Y shown below? Y (fraction saturation) 1.0 0.8 0.6 등 0.4 0.2 0.0 0 20 Oxygen binding plot 40 flog ha 60 p02 (torr) 80 100 X Y
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On the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…