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Basic Clinical Laboratory Techniques 6E

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter2: Basic Hematology

Section2.2: Hemoglobin

Problem 5RQ

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Question

Precise data have been obtained for the oxygen binding of stripped
human hemoglobin at 25 °C:
Poz
(mm Hg)
Poz
(= 100 x Yo,) (mm Hg)
% Saturation
% Saturation
(= 100 × Y)
0.10
0.315
5.75
76.0
0.350
0.990
7.94
90.9
0.794
3.06
12.88
96.9
1.748
9.09
29.51
99.0
2.884
24.0
67.60
99.7
4.467
50.0

Use a Hill plot to determine (a) Pso, (b) h (maximum slope), and (c)
the Psg values corresponding to the T and R states.

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Below is a fractional saturation curve for O₂ binding to adult hemoglobin. Assume that curve Y represents a condition at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve X represents a condition that Fractional saturation (0) 0.2 0.0 0 Tissue PO, (kPa) 12 Lungs
Below is an oxygen-binding curve for two hemoglobin variants. 1.0 0.8 0.6 B 0.4 0.2 20 40 60 80 100 O2 pressure (torr) Determine the p50 for variant A to the nearest 5 torr (i.e., if the p50 was 12, you would write 10). Determine the fraction of the hemoglobin B bound with O2 in the lungs (pO2 = 100 torr) that delivers oxygen to the tissues (pO2 = 20 torr)? Answer to the nearest 0.05 value (for example, 0.10 or 0.15). Which hemoglobin variant (write A or B or same) delivers more oxygen to tissues? Fraction bound with O2
The following data describe the binding of oxygen to human myoglobin. Posygen (mm Hg) Percent Saturation 0.5 16.1 2.0 27.7 3.0 53.5 4.0 60.5 6.0 69.7 8.0 75.4 12.0 82.1 20.0 88.5 From these data the approximate P50 (mm Hg) value is: A. 1.0 В. 1.4 С. 1.9 D. 2.6 Е. 3.2 F. 3.5 G. 3.7 Н. 3.9 I. 4.0
Figure 5 shows oxyhemoglobin dissociatlon curves at pH 7.2 and pH 7.4. Which of the following is true at PO2 less than 40 mm Hg? 27. % saturation af haemogiobin 100 pH 7.4 80 60 pH 7.2 40 + 20 10 20 30 40 50 60 70 Po; (mm Hg) Figure 5 A. Hemoglobin retains less O2 at pH 7.4 compared to pH 7.2. B. Hemoglobin retains less O2 at pH 7.2 compared to pH 7.4. C. The release of O2 from hemoglobin is not influenced by the production of CO2. D. At pH 7.2 where CO2 production is less than pH 7.4, hemoglobin releases less O2.
The arterial O₂ concentration is given by the following expression [0₂] = 0.003 P0₂ + (PO₂)².8 +(26) 2.8 1. ЗЧНЬ (Рог ) 2-8 Where Poz is the alveolar O₂ pressure and Hb is the hemoglobin concentration in g/dL, respectively A subject who is at 0-95 ATM (211-0₂) has an arterial O₂ concentration of 19ml/dL and and arterial CO₂ pressure of 38mm Hg. Also, VO₂ = 340mL/min.; VCD₂ = 289 mL/min. Therefore, your hemoglobine level is: A. 14.39 Idl 8. 14.8 g/dl C. 15.2 g/dl D. 15.7g/dL E. 16 g/dL
Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]
Suppose Gina climbs a high mountain where the oxygen partial pressure in the air decreases to 70 torr. Assume that the pH of her tissues and lungs is 7.4 and the oxygen concentration in her tissues is 20 torr. The P50 of hemoglobin is 26 torr. The degree of cooperativity of hemoglobin, n, is 2.8. Estimate the percentage of the oxygen-carrying capacity that she utilizes. Calculate your answer to one decimal place. сараcity: %
From your graph, estimate the P50 for normal hemoglobin and the mutant corresponding to your student number and explain if these results support your expectations regarding the mutant's oxygen affinity compared to normal hemoglobin. ف C Normal Yakima pO2 (torr) Yo2 Yo2 10 0.05 0.10 15 0.10 0.25 20 0.25 0.45 25 0.50 0.70 30 0.75 0.85 40 0.85 0.95 60 0.95 0.98 H
(b) The diagram on the right illustrates the change in the p50 (partial pressure of O2 required to achieve 50% saturation) of hemoglobin and the 2,3-bis-phosphoglycerate (BPG) concentration in the erythrocytes of a person who spent 6 days hik- ing in the Andes Mountains of Peru. As the hiker climbs to higher and higher altitudes, the atmos- pheric pressure, including the partial pressure of O2, decreases. Yet the p50 increases, making it less favorable to achieve saturation of the hemo- globin. Explain. Pso (torr) Sea level 34 33- 32 31 30- 29 28 27 26 4530 m above- sea level (c) If individuals with the following mutant hemo- globins accompanied the hiker, evaluate the degree of respiratory distress that they would experience despite the increased erythrocyte BPG concentration. (In the ta- ble of mutants on the right, the mutation His(143)Asp, for instance, means that the His residue that occurs at se- quence position 143 on the ß-chain has been substituted by Asp.) Describe the…
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…
2,3-bisphosphoglycerate (BPG) is a negative allosteric regulator of hemoglobin that is produced in red blood cells. Normally, red blood cell levels of BPG are 5 mmol/L, yielding curve 2. Individuals acclimated to high altitudes can have BPG levels of 8 mmol/L to optimize their oxygen utilization. Saturation 2 3 S Which curve represents hemoglobin of someone living at normal altitudes? 1 2 Pos (mm Hg) 3 None of the answers are correct 2 and 3
This graph shows the O2 binding curves of Hemoglobin. Which one is the R-state curve, and which one is the T-state? Why these curves are different comparing to the normal curve (middle one) 1.0 0.8 Observed hemoglobin- binding curve 0.6 0.4 0.2 0.0 50 100 150 200 p02 (torr) Y (fractional saturation)

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