Human Anatomy
5th Edition
ISBN: 9780073403700
Author: Kenneth S. Saladin Dr.
Publisher: McGraw-Hill Education
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Chapter 8, Problem 7TOF
Summary Introduction
To explain:
The reason humerus is not the most frequently broken bone and which one is most frequently broken bone.
Introduction:
The humerus forms the brachium of the forearm that is present between the shoulder and elbow.
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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 8 Solutions
Human Anatomy
Ch. 8.1 - Prob. 1AWYKCh. 8.1 - Describe how to distinguish the medical and...Ch. 8.1 - Prob. 2BYGOCh. 8.1 - Prob. 3BYGOCh. 8.1 - Name the carpal bones of the proximal row from...Ch. 8.1 - Name the four long bones from the tip of the...Ch. 8.1 - Palpate as many of the following structures as...Ch. 8.2 - Prob. 1AWYKCh. 8.2 - Prob. 7BYGOCh. 8.2 - Prob. 8BYGO
Ch. 8.2 - Prob. 9BYGOCh. 8.2 - Prob. 10BYGOCh. 8.2 - Name the prominent knobs on each side of your...Ch. 8.2 - Prob. 12BYGOCh. 8.2 - Prob. 13BYGOCh. 8.3 - Prob. 1BYGOCh. 8.3 - Answer the following questions to test your...Ch. 8.3 - Prob. 3BYGOCh. 8 - The function of the pectoral girdle; the bones...Ch. 8 - Prob. 8.1.2AYLOCh. 8 - The four segments (regions) of the upper limbCh. 8 - The names and locations of all 30 bones of the...Ch. 8 - The anatomical features of the humerus, radius,...Ch. 8 - How the upper limb is anatomically adapted to the...Ch. 8 - Prob. 8.2.1AYLOCh. 8 - The function of the pelvic girdle; the bones that...Ch. 8 - Prob. 8.2.3AYLOCh. 8 - Prob. 8.2.4AYLOCh. 8 - Prob. 8.2.5AYLOCh. 8 - Prob. 8.2.6AYLOCh. 8 - Prob. 8.2.7AYLOCh. 8 - Prob. 8.2.8AYLOCh. 8 - The anatomical features of the femur, patella,...Ch. 8 - Prob. 8.2.10AYLOCh. 8 - How the lower limb is adapted to the bipedalism of...Ch. 8 - What portions of the appendicular skeleton are...Ch. 8 - Prob. 8.3.2AYLOCh. 8 - Prob. 8.3.3AYLOCh. 8 - Prob. 8.3.4AYLOCh. 8 - Prob. 8.3.5AYLOCh. 8 - Prob. 1TYRCh. 8 - Prob. 2TYRCh. 8 - Prob. 3TYRCh. 8 - Prob. 4TYRCh. 8 - Prob. 5TYRCh. 8 - When you rest your hands on your hips, you are...Ch. 8 - Prob. 7TYRCh. 8 - Prob. 8TYRCh. 8 - Prob. 9TYRCh. 8 - Prob. 10TYRCh. 8 - Prob. 11TYRCh. 8 - Prob. 12TYRCh. 8 - Prob. 13TYRCh. 8 - Prob. 14TYRCh. 8 - Prob. 15TYRCh. 8 - Prob. 16TYRCh. 8 - Prob. 17TYRCh. 8 - Prob. 18TYRCh. 8 - Prob. 19TYRCh. 8 - Prob. 20TYRCh. 8 - Prob. 1BYMVCh. 8 - Prob. 2BYMVCh. 8 - Prob. 3BYMVCh. 8 - Prob. 4BYMVCh. 8 - State a meaning of each word element and give a...Ch. 8 - Prob. 6BYMVCh. 8 - Prob. 7BYMVCh. 8 - Prob. 8BYMVCh. 8 - Prob. 9BYMVCh. 8 - Prob. 10BYMVCh. 8 - Prob. 1TOFCh. 8 - Prob. 2TOFCh. 8 - Prob. 3TOFCh. 8 - Prob. 4TOFCh. 8 - Prob. 5TOFCh. 8 - Prob. 6TOFCh. 8 - Prob. 7TOFCh. 8 - Prob. 8TOFCh. 8 - Prob. 9TOFCh. 8 - Briefly explaine why each of the following...Ch. 8 - Prob. 1TYCCh. 8 - Prob. 2TYCCh. 8 - A deer hunter discovers a human skeleton in the...Ch. 8 - Prob. 4TYCCh. 8 - Andy, a 55-year-old, 75 kg (165-pound) roofer, is...
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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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