Human Physiology
15th Edition
ISBN: 9781259864629
Author: Fox, Stuart Ira
Publisher: Mcgraw-hill Education,
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Chapter 12, Problem 2RA
Summary Introduction
To determine:
Role of series elastic component of muscle contraction.
Introduction:
Muscle contraction involves various factors such as calcium ion, troponin, and tropomyosin. Muscle contraction takes place in the following steps: Depolarisation and release of calcium ions, actin and myosin cross-bridge formation, sliding mechanism of actin filaments, and myosin and sarcomere shortening.
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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?
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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 12 Solutions
Human Physiology
Ch. 12 - Describe the actions of muscles when they...Ch. 12 - Describe the different levels of muscle structure,...Ch. 12 - Define the terms motor unit and innervation ratio...Ch. 12 - Using the concept of recruitment, explain how...Ch. 12 - With reference to the sliding filament theory,...Ch. 12 - Prob. 3bCPCh. 12 - Describe a cycle of cross-bridge activity during...Ch. 12 - Prob. 4bCPCh. 12 - Use a flowchart to show the sequence of events...Ch. 12 - Prob. 5bCP
Ch. 12 - Explain how graded contractions and smooth,...Ch. 12 - Prob. 6bCPCh. 12 - Prob. 7aCPCh. 12 - Describe the relationship between the resting...Ch. 12 - Prob. 8CPCh. 12 - Prob. 9CPCh. 12 - Explain the different causes of muscle fatigue...Ch. 12 - Prob. 11CPCh. 12 - Prob. 12aCPCh. 12 - Describe all of the events that occur from the...Ch. 12 - Prob. 13CPCh. 12 - Explain the significance of reciprocal innervation...Ch. 12 - Describe the functions of gamma motor neurons and...Ch. 12 - Explain how cardiac muscle differs from skeletal...Ch. 12 - Contrast the structure of a smooth muscle cell...Ch. 12 - Distinguish between single-unit and multiunit...Ch. 12 - Describe the events by which depolarization of a...Ch. 12 - Prob. 1RACh. 12 - Prob. 2RACh. 12 - Prob. 3RACh. 12 - Prob. 4RACh. 12 - Prob. 5RACh. 12 - Prob. 6RACh. 12 - Prob. 7RACh. 12 - Electrical excitation of a muscle fiber most...Ch. 12 - The energy for muscle contraction is most directly...Ch. 12 - Prob. 10RACh. 12 - Prob. 11RACh. 12 - Prob. 12RACh. 12 - Which of these types of muscle cells are not...Ch. 12 - Prob. 14RACh. 12 - In an isotonic muscle contraction,...Ch. 12 - Prob. 16RACh. 12 - Prob. 17RACh. 12 - Prob. 18RACh. 12 - Using the concept of motor units, explain how...Ch. 12 - Prob. 20RACh. 12 - Explain why the myosin heads don't bind to the...Ch. 12 - Using the sliding filament theory of contraction,...Ch. 12 - Prob. 23RACh. 12 - Prob. 24RACh. 12 - Prob. 25RACh. 12 - What changes occur in muscle metabolism as the...Ch. 12 - Prob. 27RACh. 12 - Compare cardiac muscle, single-unit smooth muscle,...Ch. 12 - Your friend eats huge helpings or pasta for two...Ch. 12 - Prob. 30RACh. 12 - Prob. 31RACh. 12 - How is electrical excitation of a skeletal muscle...Ch. 12 - Prob. 33RACh. 12 - Prob. 34RACh. 12 - Prob. 35RACh. 12 - Prob. 36RACh. 12 - Refer to figure 12.22 to answer the following...Ch. 12 - Refer to figure 12.22 to answer the following...Ch. 12 - Prob. 39RACh. 12 - Refer to figure 12.22 to answer the following...
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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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