FUNDAMENTALS OF ANATOMY AND PHYSIOLOGY
11th Edition
ISBN: 2818440070938
Author: Martini
Publisher: PEARSON C
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Chapter 24, Problem 2CC
Summary Introduction
To determine:
The observation of the colonoscopy of Mirasol, when she is diagnosed with Clostridium difficile colitis
Introduction:
Clostridium difficile colitis is the result of eroded natural microflora of the intestine due to overuse of antibiotics by the body. The new habitants of the intestine are generally harmful to the intestine and they create irritation and produces toxins that might harm the body.
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Chapter 24 Solutions
FUNDAMENTALS OF ANATOMY AND PHYSIOLOGY
Ch. 24 - Prob. 1CPCh. 24 - Prob. 2CPCh. 24 - Prob. 3CPCh. 24 - Prob. 4CPCh. 24 - Name the layers of the gastrointestinal tract...Ch. 24 - Which is more efficient in propelling intestinal...Ch. 24 - Prob. 7CPCh. 24 - Prob. 8CPCh. 24 - Prob. 9CPCh. 24 - Prob. 10CP
Ch. 24 - Prob. 11CPCh. 24 - Prob. 12CPCh. 24 - Prob. 13CPCh. 24 - Name the structure connecting the pharynx to the...Ch. 24 - Prob. 15CPCh. 24 - Identify the muscles associated with the pharynx...Ch. 24 - What is occurring when the soft palate and larynx...Ch. 24 - Name the four major regions of the stomach.Ch. 24 - Prob. 19CPCh. 24 - Prob. 20CPCh. 24 - Prob. 21CPCh. 24 - The digestion of which nutrient would be most...Ch. 24 - Prob. 23CPCh. 24 - Prob. 24CPCh. 24 - Name the three regions of the small intestine from...Ch. 24 - Prob. 26CPCh. 24 - Prob. 27CPCh. 24 - How would the pH of the intestinal contents be...Ch. 24 - Prob. 29CPCh. 24 - Name some major histological differences between...Ch. 24 - Prob. 31CPCh. 24 - Prob. 32CPCh. 24 - Prob. 33CPCh. 24 - Prob. 34CPCh. 24 - Prob. 35CPCh. 24 - Prob. 36CPCh. 24 - Prob. 37CPCh. 24 - What body systems may be affected by inadequate...Ch. 24 - The enzymatic breakdown of large molecules into...Ch. 24 - Prob. 2RQCh. 24 - Prob. 3RQCh. 24 - Prob. 4RQCh. 24 - Prob. 5RQCh. 24 - Prob. 6RQCh. 24 - Prob. 7RQCh. 24 - Prob. 8RQCh. 24 - Prob. 9RQCh. 24 - Prob. 10RQCh. 24 - Prob. 11RQCh. 24 - Prob. 12RQCh. 24 - Prob. 13RQCh. 24 - Prob. 14RQCh. 24 - Prob. 15RQCh. 24 - What three basic mechanisms regulate the...Ch. 24 - Prob. 17RQCh. 24 - What are the primary digestive functions of the...Ch. 24 - Prob. 19RQCh. 24 - What are the three primary functions of the large...Ch. 24 - What two positive feedback loops are involved in...Ch. 24 - Prob. 22RQCh. 24 - Prob. 23RQCh. 24 - Prob. 24RQCh. 24 - Through which layers of a molar would an oral...Ch. 24 - Prob. 26RQCh. 24 - Prob. 27RQCh. 24 - Prob. 28RQCh. 24 - Some people with gallstones develop pancreatitis....Ch. 24 - Prob. 30RQCh. 24 - A condition known as lactose intolerance is...Ch. 24 - Prob. 32RQCh. 24 - Prob. 1CCCh. 24 - Prob. 2CC
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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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