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11th Edition
ISBN: 9781259807657
Author: Cinnamon VanPutte, Jennifer Regan, Andrew F. Russo Dr., Rod R. Seeley Dr.
Publisher: MCGRAW-HILL HIGHER EDUCATION
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Chapter 19.6, Problem 44AYP
Summary Introduction
To analyze:
The reason due to which HDN (hemolytic disease of newborns) does not take place after the first pregnancy.
Introduction:
Hemolytic disease results in the excessive destruction of the red blood cells in the spleen, which causes a lack of red blood cells in the blood leading to the development of anemia. The reticulocyte count that is the precursor of erythrocyte increase in hemolytic disease as a large number of erythrocyte precursors is released into the blood to compensate for the loss of red blood cells.
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A sample of blood was taken from the above individual and prepared for haemoglobin analysis. However, when water was added the cells did not lyse and looked normal in size and shape. The technician suspected that they had may have made an error in the protocol – what is the most likely explanation?
The cell membranes are more resistant than normal.
An isotonic solution had been added instead of water.
A solution of 0.1 M NaCl had been added instead of water.
Not enough water had been added to the red blood cell pellet.
The man had sickle-cell anaemia.
A sample of blood was taken from the above individual and prepared for haemoglobin analysis. However, when water was added the cells did not lyse and looked normal in size and shape. The technician suspected that they had may have made an error in the protocol – what is the most likely explanation?
The cell membranes are more resistant than normal.
An isotonic solution had been added instead of water.
A solution of 0.1 M NaCl had been added instead of water.
Not enough water had been added to the red blood cell pellet.
The man had sickle-cell anaemia.
With reference to their absorption spectra of the oxy haemoglobin intact line) and deoxyhemoglobin (broken line) shown in Figure 2 below, how would you best explain the reason why there are differences in the major peaks of the spectra? Figure 2. SPECTRA OF OXYGENATED AND DEOXYGENATED HAEMOGLOBIN OBTAINED WITH THE RECORDING SPECTROPHOTOMETER 1.4 Abs < 0.8 06 0.4 400 420 440 460 480 500 520 540 560 580 600 nm 1. The difference in the spectra is due to a pH change in the deoxy-haemoglobin due to uptake of CO2- 2. There is more oxygen-carrying plasma in the oxy-haemoglobin sample. 3. The change in Mr due to oxygen binding causes the oxy haemoglobin to have a higher absorbance peak. 4. Oxy-haemoglobin is contaminated by carbaminohemoglobin, and therefore has a higher absorbance peak 5. Oxy-haemoglobin absorbs more light of blue wavelengths and less of red wavelengths than deoxy-haemoglobin
Chapter 19 Solutions
Connect with LearnSmart Labs Access Card for Seeley's A&P
Ch. 19.1 - List the ways that blood helps maintain...Ch. 19.1 - Prob. 2AYPCh. 19.1 - What is the normal pH range of the blood?Ch. 19.1 - Prob. 4AYPCh. 19.2 - Prob. 5AYPCh. 19.2 - Prob. 6AYPCh. 19.3 - Prob. 7AYPCh. 19.3 - Prob. 8AYPCh. 19.3 - Explain how plasma volume remains relatively...Ch. 19.4 - Name the three general types of formed elements in...
Ch. 19.4 - Prob. 11AYPCh. 19.4 - What types of formed elements develop from each of...Ch. 19.4 - Prob. 13AYPCh. 19.4 - Prob. 14AYPCh. 19.4 - Prob. 15AYPCh. 19.4 - Prob. 16AYPCh. 19.4 - Prob. 17AYPCh. 19.4 - Prob. 18AYPCh. 19.4 - Prob. 19AYPCh. 19.4 - Prob. 20AYPCh. 19.4 - Prob. 21AYPCh. 19.4 - Prob. 22AYPCh. 19.4 - Describe the morphology of the five types of white...Ch. 19.4 - Prob. 24AYPCh. 19.4 - Prob. 25AYPCh. 19.4 - Prob. 26AYPCh. 19.4 - Prob. 27AYPCh. 19.4 - What is a platelet? How do platelets form?Ch. 19.4 - Prob. 29AYPCh. 19.5 - Prob. 30AYPCh. 19.5 - What is the function of a platelet plug? Describe...Ch. 19.5 - Prob. 32AYPCh. 19.5 - Prob. 33AYPCh. 19.5 - Prob. 34AYPCh. 19.5 - Prob. 35AYPCh. 19.5 - Prob. 36AYPCh. 19.5 - Prob. 37AYPCh. 19.5 - Prob. 38AYPCh. 19.6 - Prob. 39AYPCh. 19.6 - Prob. 40AYPCh. 19.6 - Prob. 41AYPCh. 19.6 - Prob. 42AYPCh. 19.6 - Prob. 43AYPCh. 19.6 - Prob. 44AYPCh. 19.7 - What occurs in a type and crossmatch?Ch. 19.7 - Prob. 46AYPCh. 19.7 - Prob. 47AYPCh. 19.7 - Prob. 48AYPCh. 19 - Prob. 1RACCh. 19 - Prob. 2RACCh. 19 - Prob. 3RACCh. 19 - Prob. 4RACCh. 19 - Prob. 5RACCh. 19 - Prob. 6RACCh. 19 - Prob. 7RACCh. 19 - Prob. 8RACCh. 19 - Prob. 9RACCh. 19 - Prob. 10RACCh. 19 - Prob. 11RACCh. 19 - Prob. 12RACCh. 19 - Prob. 13RACCh. 19 - Prob. 14RACCh. 19 - Prob. 15RACCh. 19 - Prob. 16RACCh. 19 - Prob. 17RACCh. 19 - Prob. 18RACCh. 19 - Prob. 19RACCh. 19 - Prob. 20RACCh. 19 - Prob. 21RACCh. 19 - Prob. 1CTCh. 19 - Prob. 2CTCh. 19 - Prob. 3CTCh. 19 - Prob. 4CTCh. 19 - Prob. 5CTCh. 19 - Prob. 6CTCh. 19 - Prob. 7CT
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- With reference to their absorption spectra of the oxy haemoglobin intact line) and deoxyhemoglobin (broken line) shown in Figure 2 below, how would you best explain the reason why there are differences in the major peaks of the spectra? Figure 2. SPECTRA OF OXYGENATED AND DEOXYGENATED HAEMOGLOBIN OBTAINED WITH THE RECORDING SPECTROPHOTOMETER 1.4 Abs < 0.8 06 0.4 400 420 440 460 480 500 520 540 560 580 600 nm 1. The difference in the spectra is due to a pH change in the deoxy-haemoglobin due to uptake of CO2- 2. There is more oxygen-carrying plasma in the oxy-haemoglobin sample. 3. The change in Mr due to oxygen binding causes the oxy haemoglobin to have a higher absorbance peak. 4. Oxy-haemoglobin is contaminated by carbaminohemoglobin, and therefore has a higher absorbance peak 5. Oxy-haemoglobin absorbs more light of blue wavelengths and less of red wavelengths than deoxy-haemoglobinarrow_forwardWhich ONE of the following is FALSE regarding haemoglobin? It has two alpha subunits and two beta subunits. The subunits are joined by disulphide bonds. Each subunit covalently binds a haem group. Conformational change in one subunit can be transmitted to another. There are many variant ("mutant") forms of haemoglobin that are not harmful.arrow_forwardWhich ONE of the following is FALSE regarding haemoglobin? It has two alpha subunits and two beta subunits. The subunits are joined by disulphide bonds. Each subunit covalently binds a haem group. Conformational change in one subunit can be transmitted to another. There are many variant ("mutant") forms of haemoglobin that are not harmful.arrow_forward
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