BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
1st Edition
ISBN: 9780134172507
Author: APPLING
Publisher: Pearson Education
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Chapter 7, Problem 4P
Interpretation Introduction
Interpretation:
The qualitative effect of each the following on the P50 of hemoglobin.
- Increase in pH from 7.2 to 7.4
- Increase in PCO2 from 20 to 40 mm Hg
- Dissociation into monomer polypeptide chains
- Decrease in 2,3-BPG concentration from 7 mM to 5mM in red cells.
Concept Introduction:
The P50 is the oxygen tension at which hemoglobin is 50% saturated. The normal P50 is 26.7 mm Hg.
Hemoglobin Dissociation Curve:
A rightward shift increases P50 and lowers hemoglobin's affinity for oxygen, thus displacing oxygen from hemoglobin and releasing it to the tissues.
A leftward shift decreases P50 and increases hemoglobin's affinity for oxygen, thus reducing its availability to the tissues.
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Fura-2 Fluorescence (Arbitrary Unit)
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[Ca2+]=2970nM, 25°C
[Ca2+] 2970nM, 4°C
[Ca2+]=0.9nM, 25°C
[Ca2+] = 0.9nM, 4°C
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Wavelength (nm)
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The figure on the LHS shows the excitation spectra of Fura-2 (Em
= 510 nm) in 2 solutions with two different Ca2+ ion concentration
as indicated. Except for temperature, the setting for excitation &
signal acquisition was identical.<
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a) The unit in Y-axis is arbitrary (unspecified). Why? <
<
b) Compare & contrast the excitation wavelength of the Isosbestic
Point of Fura-2 at 25 °C & 4 °C. Give a possible reason for the
discrepancy. <
c) The fluorescence intensity at 25 °C & 4 °C are different. Explain
why with the concept of electronic configuration. <
Chapter 7 Solutions
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