PRINCIPLES OF LIFE - LAUNCHPAD (1 TERM)
3rd Edition
ISBN: 9781319410551
Author: HILLIS
Publisher: MAC HIGHER
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Chapter 22.4, Problem 2FQ
Summary Introduction
To explain: The function of a structure that would become a wing in an insect.
Introduction: The first animals in evolutionary history to achieve the ability to fly were pterygote insects. The insects were able to exploit their flight which opened many new lifestyles and feeding opportunities to them. This was one of the reasons for unparallel evolutionary success of the insects.
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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 22 Solutions
PRINCIPLES OF LIFE - LAUNCHPAD (1 TERM)
Ch. 22.1 - Prob. 1LOCh. 22.1 - Prob. 2LOCh. 22.1 - Prob. 1FQCh. 22.1 - Prob. 1RACh. 22.1 - Prob. 2RACh. 22.1 - Prob. 3RACh. 22.1 - Prob. 4RACh. 22.2 - Prob. 1LOCh. 22.2 - Prob. 2LOCh. 22.2 - Prob. 1I
Ch. 22.2 - Prob. 2ICh. 22.2 - Prob. 3ICh. 22.2 - Prob. 4ICh. 22.2 - Prob. 1RACh. 22.2 - Prob. 2RACh. 22.2 - Prob. 3RACh. 22.3 - Prob. 1LOCh. 22.3 - Prob. 2LOCh. 22.3 - Prob. 1RACh. 22.3 - Prob. 2RACh. 22.3 - Prob. 3RACh. 22.3 - Prob. 4RACh. 22.3 - Prob. 5RACh. 22.4 - Prob. 1LOCh. 22.4 - Prob. 2LOCh. 22.4 - Prob. 3LOCh. 22.4 - Prob. 1FQCh. 22.4 - Prob. 1TKCh. 22.4 - Prob. 2TKCh. 22.4 - Prob. 3TKCh. 22.4 - Prob. 2FQCh. 22.4 - Prob. 1RACh. 22.4 - Prob. 2RACh. 22.4 - Prob. 3RACh. 22.5 - Prob. 1LOCh. 22.5 - Prob. 2LOCh. 22.5 - Prob. 3LOCh. 22.5 - Prob. 4LOCh. 22.5 - Prob. 1RACh. 22.5 - Prob. 2RACh. 22.5 - Prob. 3RACh. 22.5 - Prob. 4RACh. 22.5 - Prob. 5RACh. 22.6 - Prob. 1LOCh. 22.6 - Prob. 2LOCh. 22.6 - Prob. 3LOCh. 22.6 - Prob. 4LOCh. 22.6 - Prob. 1FQCh. 22.6 - Prob. 2FQCh. 22.6 - Prob. 1RACh. 22.6 - Prob. 2RACh. 22.6 - Prob. 3RACh. 22.6 - Prob. 4RACh. 22.7 - Prob. 1LOCh. 22.7 - Prob. 2LOCh. 22.7 - Prob. 1RACh. 22.7 - Prob. 2RACh. 22 - Prob. 1.1QCh. 22 - Prob. 1.2QCh. 22 - Prob. 1.3QCh. 22 - Prob. 2.1QCh. 22 - Prob. 2.2QCh. 22 - Prob. 3.1QCh. 22 - Prob. 3.2QCh. 22 - Prob. 4.1QCh. 22 - Prob. 4.2QCh. 22 - Prob. 5.1QCh. 22 - Prob. 5.2QCh. 22 - Prob. 6.1QCh. 22 - Prob. 6.2QCh. 22 - Prob. 6.3QCh. 22 - Prob. 7.1QCh. 22 - Prob. 7.2Q
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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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