VANDER'S HUMAN PHYS CONNECT ACC/PROCT+
15th Edition
ISBN: 9781265160821
Author: WIDMAIER
Publisher: MCG
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Chapter 9, Problem A.26RQ
Summary Introduction
To determine: The factors that affect the amount of tension developed by a whole skeletal muscle depend.
Introduction: In an adult, 40 to 50% body weight is contributed by skeletal muscles. The primary cells that form a skeletal muscle is the skeletal muscle fibers. They perform functions such as body movement, posture maintenance, support and protection, heat production, and regulating elimination of materials.
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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 9 Solutions
VANDER'S HUMAN PHYS CONNECT ACC/PROCT+
Ch. 9 - Prob. 1PICh. 9 - Prob. 2PICh. 9 - If the ACh receptor channel is equally permeable...Ch. 9 - Prob. 4PICh. 9 - Prob. 5PICh. 9 - Under certain experimental conditions, it is...Ch. 9 -
Figure 9.16 (a) Measurement of tension during a...Ch. 9 - Prob. 8PICh. 9 - Prob. 9PICh. 9 - Prob. 10PI
Ch. 9 - Prob. 11PICh. 9 - Prob. 12PICh. 9 - Prob. 13PICh. 9 - List the three types of muscle cells and their...Ch. 9 - Prob. A.2RQCh. 9 - Describe the organization of myosin, actin,...Ch. 9 - Prob. A.4RQCh. 9 - Describe the structure and function of the...Ch. 9 - Define motor unit and describe its structure.
Ch. 9 - Describe the sequence of events by which an action...Ch. 9 - What is an end-plate potential, and what ions...Ch. 9 - Prob. A.9RQCh. 9 - What prevents cross-bridges from attaching to...Ch. 9 - Prob. A.11RQCh. 9 - Prob. A.12RQCh. 9 - Prob. A.13RQCh. 9 - Prob. A.14RQCh. 9 - Prob. A.15RQCh. 9 - Describe isometric, concentric, and eccentric...Ch. 9 - Prob. A.17RQCh. 9 - Prob. A.18RQCh. 9 - Prob. A.19RQCh. 9 - Prob. A.20RQCh. 9 - Prob. A.21RQCh. 9 - What fuel molecules are metabolized to produce ATP...Ch. 9 - Prob. A.23RQCh. 9 - What component of skeletal muscle fibers accounts...Ch. 9 - Summarize the characteristics of the three types...Ch. 9 - Prob. A.26RQCh. 9 - Prob. A.27RQCh. 9 - Prob. A.28RQCh. 9 - Prob. A.29RQCh. 9 - Prob. A.30RQCh. 9 - Prob. A.31RQCh. 9 - Prob. A.32RQCh. 9 - Prob. 14PICh. 9 - Prob. B.1RQCh. 9 - Prob. B.2RQCh. 9 - Prob. B.3RQCh. 9 - Prob. B.4RQCh. 9 - Prob. B.5RQCh. 9 - Prob. B.6RQCh. 9 - Prob. B.7RQCh. 9 - Prob. B.8RQCh. 9 - Prob. B.9RQCh. 9 - Explain why cardiac muscle cannot undergo tetanic...Ch. 9 - Prob. 1RRCh. 9 - Prob. 2RRCh. 9 - Prob. 1RCCh. 9 - Prob. 2RCCh. 9 - Prob. 3RCCh. 9 - Prob. 4RCCh. 9 - Prob. 5RCCh. 9 - Prob. 6RCCh. 9 - Prob. 7RCCh. 9 - Prob. 8RCCh. 9 - Prob. 9RCCh. 9 - Prob. 10RCCh. 9 - Prob. 11RCCh. 9 - Prob. 1AAECh. 9 - Prob. 2AAECh. 9 - Prob. 3AAECh. 9 - Prob. 4AAECh. 9 - Prob. 5AAECh. 9 - Prob. 6AAECh. 9 - Prob. 7AAECh. 9 - Prob. 8AAECh. 9 -
If a single twitch of a skeletal muscle fiber...Ch. 9 - Prob. 10AAECh. 9 - Prob. 1GPACh. 9 - Prob. 2GPACh. 9 - Prob. 3GPA
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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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