ANATOMY AND PHYSIOLOGY
4th Edition
ISBN: 9781265506605
Author: Bidle
Publisher: MCG
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Chapter 10.5, Problem 20WDYL
Summary Introduction
To determine:
The type of the muscle fiber that is slow and fatigue resistant and also the advantage of this muscle fiber type.
Concept introduction:
Oxidative fibers specialize in providing energy (ATP) by aerobic
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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 10 Solutions
ANATOMY AND PHYSIOLOGY
Ch. 10.1 - What are the five major functions of skeletal...Ch. 10.1 - Prob. 2WDYLCh. 10.2 - Prob. 3WDYLCh. 10.2 - Draw and label a diagram of a sarcomere.Ch. 10.2 - Prob. 5WDYLCh. 10.2 - Prob. 6WDYLCh. 10.2 - Diagram and label the anatomic structures of a...Ch. 10.2 - Prob. 8WDYLCh. 10.3 - What triggers the binding of synaptic vesicles to...Ch. 10.3 - What two events are linked in the physiologic...
Ch. 10.3 - Prob. 11WDYLCh. 10.3 - Prob. 12WDYLCh. 10.3 - Describe the four processes that repeat in...Ch. 10.3 - What causes the release of the myosin head from...Ch. 10.3 - How do acetylcholinesterase and Ca2+ pumps...Ch. 10.4 - Prob. 16WDYLCh. 10.4 - What are the various means for making ATP...Ch. 10.4 - Prob. 18WDYLCh. 10.5 - Prob. 19WDYLCh. 10.5 - Prob. 20WDYLCh. 10.5 - Prob. 21WDYLCh. 10.6 - What events are occurring in a muscle that produce...Ch. 10.6 - What is recruitment? Explain its importance in the...Ch. 10.6 - Prob. 24WDYLCh. 10.7 - What is the function of skeletal muscle tone?Ch. 10.7 - When you flex your biceps brachii while doing...Ch. 10.7 - Prob. 27WDYLCh. 10.7 - How can muscle fatigue result from changes in each...Ch. 10.8 - Prob. 29WDYLCh. 10.8 - Prob. 30WDYLCh. 10.9 - What are three anatomic or physiologic differences...Ch. 10.10 - Prob. 32WDYLCh. 10.10 - Prob. 33WDYLCh. 10.10 - Prob. 34WDYLCh. 10.10 - What are the steps of smooth muscle contraction?Ch. 10.10 - What unique characteristics of smooth muscle allow...Ch. 10.10 - Prob. 37WDYLCh. 10.10 - Prob. 38WDYLCh. 10.10 - Prob. 39WDYLCh. 10 - Prob. 1DYKBCh. 10 - The physiologic event that takes place at the...Ch. 10 - In a skeletal muscle fiber, Ca2+ is released from...Ch. 10 - The bundle of dense regular connective tissue that...Ch. 10 - In excitation-contraction coupling, the transverse...Ch. 10 - During muscle contraction, the I band a. hides the...Ch. 10 - During a concentric contraction of a muscle fiber,...Ch. 10 - What event causes a troponin-tropomyosin complex...Ch. 10 - In sustained, moderate exercise, skeletal muscle...Ch. 10 - Skeletal muscle and cardiac muscle are similar in...Ch. 10 - Explain the structural relationship between a...Ch. 10 - Prob. 12DYKBCh. 10 - Prob. 13DYKBCh. 10 - Put the following skeletal muscle contraction...Ch. 10 - Explain the various means of providing ATP for...Ch. 10 - Explain why athletes who excel at short sprints...Ch. 10 - Explain why skeletal muscle generates the most...Ch. 10 - Prob. 18DYKBCh. 10 - Describe the response of smooth muscle to...Ch. 10 - Prob. 20DYKBCh. 10 - Prob. 1CALCh. 10 - One of the primary reasons that one individual is...Ch. 10 - Prob. 3CALCh. 10 - Rigor mortis occurs following death because a....Ch. 10 - Prob. 5CALCh. 10 - Prob. 1CSLCh. 10 - Describe the effect of the botulinum toxin, which...Ch. 10 - Smooth muscle is within the urinary bladder wall....
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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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