Prescott's Microbiology
10th Edition
ISBN: 9781259281594
Author: Joanne Willey, Linda Sherwood Adjunt Professor Lecturer, Christopher J. Woolverton Professor
Publisher: McGraw-Hill Education
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Chapter 41.3, Problem 3RIA
Summary Introduction
Aflatoxins are ringed and planar compounds. They intercalate between strands of deoxyribonucleic acids (DNA), causing cancer due to the frameshift mutation. Liver is the main site for these reactions where aflatoxins form unstable derivatives.
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Chapter 41 Solutions
Prescott's Microbiology
Ch. 41.1 - What are some intrinsic factors that influence...Ch. 41.1 - How would the spoilage of bread differ from that...Ch. 41.1 - Why do sausage and other ground meat products...Ch. 41.1 - What extrinsic factors can determine whether food...Ch. 41.2 - MICRO INQUIRY Canned products such as vegetable...Ch. 41.2 - Describe the major approaches used in food...Ch. 41.2 - What types of chemicals can be used to preserve...Ch. 41.2 - What cellular component does HHP target? What is...Ch. 41.2 - How does nisin function? What bacterial genus...Ch. 41.2 - Prob. 5RIA
Ch. 41.2 - What are the major gases involved in MAP? How are...Ch. 41.3 - MICRO INQUIRY What foods are most prone to...Ch. 41.3 - What is the difference between a food-borne...Ch. 41.3 - What practical recommendations regarding food...Ch. 41.3 - Prob. 3RIACh. 41.3 - Members of what microbial genus produce fumonisins...Ch. 41.4 - MICRO INQUIRY Why is it important that PulseNet...Ch. 41.4 - How are most food-borne pathogens detected?Ch. 41.4 - Why is it advantageous to omit the pre-enrichment...Ch. 41.4 - How is PulseNet used in the surveillance of...Ch. 41.4 - How are most food-borne pathogens detected?Ch. 41.5 - Can you name at least two features that make these...Ch. 41.5 - What are the major types of milk fermentations?Ch. 41.5 - What are the major types of milk fermentations?Ch. 41.5 - What major steps are used to produce cheese? How...Ch. 41.5 - Prob. 1.4RIACh. 41.5 - Describe and contrast the processes of wine and...Ch. 41.5 - How do champagnes differ from wines?Ch. 41.5 - Describe how distilled spirits such as whiskey are...Ch. 41.5 - What microorganisms are most important in...Ch. 41.6 - What bacterial genera are often included in...Ch. 41.6 - How are probiotics used in agriculture?Ch. 41 - Compare the sell-by date of a package of hot dogs...Ch. 41 - You are going through a salad line in a cafeteria...Ch. 41 - Why were aflatoxins not discovered before the...Ch. 41 - What advantage might the Shiga-like toxin give E....Ch. 41 - Keep a record of what you eat for a day or two....Ch. 41 - During cheese production, LAB convert lactose to...Ch. 41 - Following recent outbreaks of E. coli O157:H7...
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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.arrow_forwardA 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.arrow_forwardWith 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_forward
- 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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