PRESCOTT'S MICROBIOLOGY
11th Edition
ISBN: 2818440045677
Author: WILLEY
Publisher: MCG
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Chapter 3.6, Problem 4CC
Summary Introduction
To explain: The importance of conjugative plasmid, R plasmid, Col plasmid, and virulence plasmid.
Introduction: A plasmid is a small, extrachromosomal DNA molecule within a cell. It physically separates from chromosomal DNA and it can replicate independently. In bacteria, the plasmids are most commonly found as a small circular, double-stranded DNA molecule. However, sometimes plasmids are present in eukaryotic organisms and archaea.
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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 3 Solutions
PRESCOTT'S MICROBIOLOGY
Ch. 3.2 - Retrieve, Infer, Apply Why is the term prokaryote...Ch. 3.2 - Retrieve, Infer, Apply What characteristic shapes...Ch. 3.2 - Retrieve, Infer, Apply What advantages might a...Ch. 3.2 - Prob. 4CCCh. 3.3 - Retrieve, Infer, Apply List the functions of...Ch. 3.3 - Prob. 2CCCh. 3.3 - Retrieve, Infer, Apply 3. On what basis are...Ch. 3.3 - Retrieve, Infer, Apply Describe facilitated...Ch. 3.3 - Retrieve, Infer, Apply 5. What are uniport,...Ch. 3.3 - Retrieve, Infer, Apply 6. What are siderophores?...
Ch. 3.4 - MICRO INQUIRY How does the outer membrane of the...Ch. 3.4 - MICRO INQUIRY Are these transporter proteins...Ch. 3.4 - Retrieve, Infer, Apply Describe in detail the...Ch. 3.4 - Retrieve, Infer, Apply When protoplasts and...Ch. 3.4 - Retrieve, Infer, Apply 4. The cell walls of most...Ch. 3.4 - Retrieve, Infer, Apply What two mechanisms allow...Ch. 3.5 - Retrieve, Infer, Apply What is the difference...Ch. 3.5 - Retrieve, Infer, Apply S-layers and some capsules...Ch. 3.6 - Retrieve, Infer, Apply Briefly describe the nature...Ch. 3.6 - Retrieve, Infer, Apply List the most common kinds...Ch. 3.6 - Retrieve, Infer, Apply do plasmids differ from...Ch. 3.6 - Prob. 4CCCh. 3.7 - MICRO INQUIRY How does flagellum growth compare to...Ch. 3.7 - Retrieve, Infer, Apply What are the functions of...Ch. 3.7 - Retrieve, Infer, Apply What terms are used to...Ch. 3.7 - Retrieve, Infer, Apply What is self-assembly? Why...Ch. 3.8 - Would this flagellum be found in a typical...Ch. 3.8 - Retrieve, Infer, Apply Describe the way many...Ch. 3.8 - Prob. 2CCCh. 3.8 - Prob. 3CCCh. 3.8 - Retrieve, Infer, Apply Suggest why chemotaxis is...Ch. 3.9 - Retrieve, Infer, Apply Describe the structure of...Ch. 3.9 - Retrieve, Infer, Apply Briefly describe endospore...Ch. 3.9 - Retrieve, Infer, Apply What features of the...Ch. 3 - Prob. 1RCCh. 3 - Prob. 2RCCh. 3 - Prob. 3RCCh. 3 - Propose a model for the assembly of a flagellum in...Ch. 3 - The peptidoglycan of bacteria has been compared...Ch. 3 - Why might a microbe have more than one uptake...Ch. 3 - Prob. 4ALCh. 3 - What would you expect to observe if you were able...Ch. 3 - Develop a hypothesis to explain why gas vacuoles...Ch. 3 - Prob. 7AL
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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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