
Concepts of Biology
1st Edition
ISBN: 9781938168116
Author: Samantha Fowler, Rebecca Roush, James Wise
Publisher: OpenStax College
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Chapter 12, Problem 17CTQ
How does a biologist determine the polarity of a character change?
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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 12 Solutions
Concepts of Biology
Ch. 12 - Figure 12.3 In what levels are cats and dogs...Ch. 12 - Figure 12.8 Which animals in this figure belong to...Ch. 12 - What is a phylogeny a description of? a. mutations...Ch. 12 - What do scientists in the field of systematics...Ch. 12 - Which statement about the taxonomic classification...Ch. 12 - Which best describes the relationship between...Ch. 12 - Which best describes a branch point in a...Ch. 12 - Which statement about analogies is correct? a....Ch. 12 - What kind of trait is important to cladistics? a....Ch. 12 - What is true about organisms that are a part of...
Ch. 12 - Which assumption of cladistics is stated...Ch. 12 - A monophyletic group is a ______. a. phylogenetic...Ch. 12 - How does a phylogenetic tree indicate major...Ch. 12 - List the different levels of the taxonomic...Ch. 12 - Dolphins and fish have similar body shapes. Is...Ch. 12 - Describe maximum parsimony.Ch. 12 - How does a biologist determine the polarity of a...
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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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