HUMAN BIOLOGY (LOOSELEAF)
16th Edition
ISBN: 9781260482690
Author: Mader
Publisher: MCG
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Chapter 6.4, Problem 2BTH
Summary Introduction
To determine:
The medical condition in which aspirin should not be used.
Concept introduction:
Blood clot formation inhibits blood bleeding in damaged vessel. In blood clotting pathways several factors or proteins are important in clot formation like prothrombin which convert into thrombin, fibrinogen which form fibrin network, vitamin K essential in production of clotting factor or Ca2+
There are chances of clot dislodge or clot formation at another site which increase the risk of stroke. To reduce the stroke risk or inhibit the random clot formation, antiplatelet like aspirin or anticoagulants like heparin are used.
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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 6 Solutions
HUMAN BIOLOGY (LOOSELEAF)
Ch. 6.1 - List the functions of blood in the human body.Ch. 6.1 - Prob. 2LOCh. 6.1 - Describe the composition of plasma.Ch. 6.1 - Summarize the components of blood.Ch. 6.1 - Prob. 2CYPCh. 6.1 - List the types of plasma proteins and explain why...Ch. 6.2 - Prob. 1LOCh. 6.2 - Prob. 2LOCh. 6.2 - Prob. 3LOCh. 6.2 - Prob. 1CYP
Ch. 6.2 - Prob. 2CYPCh. 6.2 - Prob. 3CYPCh. 6.3 - Prob. 1LOCh. 6.3 - Prob. 2LOCh. 6.3 - Prob. 3LOCh. 6.3 - Prob. 1CYPCh. 6.3 - Prob. 2CYPCh. 6.3 - Prob. 3CYPCh. 6.4 - Prob. 1LOCh. 6.4 - Prob. 2LOCh. 6.4 - Describe disorders associated with blood clotting.Ch. 6.4 - If you were a medical researcher, what other areas...Ch. 6.4 - Prob. 2BTHCh. 6.4 - Prob. 1CYPCh. 6.4 - Prob. 2CYPCh. 6.4 - Summarize a few of the blood-clotting disorders.Ch. 6.5 - Prob. 1LOCh. 6.5 - Prob. 2LOCh. 6.5 - 3.Summarize the role of Rh factor in hemolytic...Ch. 6.5 - Prob. 1BTHCh. 6.5 - Are there other risk factors you think should be...Ch. 6.5 - Prob. 1CYPCh. 6.5 - Prob. 2CYPCh. 6.5 - Prob. 3CYPCh. 6.6 - Summarize how the cardiovascular system interacts...Ch. 6.6 - Prob. 1CYPCh. 6 - Prob. 1ACh. 6 - Prob. 2ACh. 6 - Prob. 3ACh. 6 - Prob. 4ACh. 6 - Prob. 5ACh. 6 - Prob. 6ACh. 6 - Key:
a. lymphocytes
b. monocyte
c. neutrophils
d....Ch. 6 - Prob. 8ACh. 6 - Prob. 9ACh. 6 - Prob. 10ACh. 6 - Prob. 11ACh. 6 - Prob. 12ACh. 6 - Prob. 13ACh. 6 - Prob. 14ACh. 6 - Prob. 15ACh. 6 - Prob. 16ACh. 6 - Prob. 1TCCh. 6 - Prob. 2TCCh. 6 - Prob. 3TCCh. 6 - Prob. 4TCCh. 6 - Athletes who abuse erythropoietin have many more...Ch. 6 - Prob. 6TC
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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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