
Foundations in Microbiology
10th Edition
ISBN: 9781259705212
Author: Kathleen Park Talaro, Barry Chess Instructor
Publisher: McGraw-Hill Education
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Textbook Question
Chapter 17.3, Problem 8ELO
Explain the different variations on genetic testing and how they can be used in identification and diagnosis.
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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 17 Solutions
Foundations in Microbiology
Ch. 17.1 - Describe what is involved in the main categories...Ch. 17.1 - Explain several techniques in specimen collection...Ch. 17.1 - Summarize the main procedures in isolation,...Ch. 17.1 - Summarize the major techniques in identifying and...Ch. 17.1 - Describe the general principles in specimen...Ch. 17.1 - Explain why it is important to prevent microbes...Ch. 17.1 - Summarize the kinds of tests that are used to...Ch. 17.2 - Describe some direct methods of testing a...Ch. 17.2 - Summarize the aims in selection of culture...Ch. 17.2 - Prob. 6ELO
Ch. 17.2 - Describe how flowcharts and comparison tables are...Ch. 17.3 - Explain the different variations on genetic...Ch. 17.3 - Describe what is involved in direct specimen...Ch. 17.3 - Prob. 6CYPCh. 17.3 - Describe the applications of PCR in identification...Ch. 17.4 - Describe the background aims of immunologic...Ch. 17.4 - Identify how antigen-antibody reactions are...Ch. 17.4 - Prob. 11ELOCh. 17.4 - Explain the basic methods behind the Western blot...Ch. 17.4 - Prob. 13ELOCh. 17.4 - What is the basis of serology and serological...Ch. 17.4 - Differentiate between specificity and sensitivity.Ch. 17.4 - Prob. 10CYPCh. 17.4 - Prob. 11CYPCh. 17.4 - Prob. 12CYPCh. 17.4 - Prob. 13CYPCh. 17.4 - Give examples of several tests that employ...Ch. 17.4 - What is meant by complement fixation? What are...Ch. 17.4 - Prob. 16CYPCh. 17.5 - Describe the concepts behind the main types of...Ch. 17.5 - Prob. 15ELOCh. 17.6 - Prob. 16ELOCh. 17.6 - Prob. 17CYPCh. 17.6 - Prob. 18CYPCh. 17.6 - Prob. 19CYPCh. 17.6 - Prob. 20CYPCh. 17.6 - Observing figure 17.17, indicate whether each...Ch. 17.L1 - Multiple Matching. Match each of the following...Ch. 17.L1 - Prob. 2MCQCh. 17.L1 - Prob. 3MCQCh. 17.L1 - Prob. 4MCQCh. 17.L1 - A patient with a _____ titer of antibodies to an...Ch. 17.L1 - Prob. 6MCQCh. 17.L1 - Prob. 7MCQCh. 17.L1 - An example of an in vivo serological test is a....Ch. 17.L1 - Which of the following specimens must be removed...Ch. 17.L1 - Prob. 1CSRCh. 17.L1 - Prob. 2CSRCh. 17.L1 - Prob. 3CSRCh. 17.L1 - Prob. 1WCCh. 17.L1 - Prob. 2WCCh. 17.L1 - Briefly describe the principles and give an...Ch. 17.L1 - Prob. 4WCCh. 17.L1 - Prob. 5WCCh. 17.L1 - Prob. 6WCCh. 17.L2 - Prob. 1CTCh. 17.L2 - Prob. 2CTCh. 17.L2 - Why do some tests for antibody in serum (such as...Ch. 17.L2 - Prob. 4CTCh. 17.L2 - Prob. 5CTCh. 17.L2 - Prob. 6CTCh. 17.L2 - From chapter 3, fig 3.17a (reproduced on the...Ch. 17.L2 - Prob. 2VC
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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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