LSC TOMBALL BIOLOGY CONNECT ACCESS
14th Edition
ISBN: 9781265728496
Author: Mader
Publisher: MCG CUSTOM
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Chapter 2, Problem 3A
Summary Introduction
Introduction:
The hydrogen bond is developed due to the electrostatic attraction between two polar molecules that forms when a hydrogen atom of one polar molecule (water) covalently bound to an electronegative atom (like oxygen, nitrogen, or fluorine) in typically same or another polar molecule.
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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 2 Solutions
LSC TOMBALL BIOLOGY CONNECT ACCESS
Ch. 2.1 - Prob. 1LOCh. 2.1 - Prob. 2LOCh. 2.1 - Prob. 3LOCh. 2.1 - Identify the beneficial and harmful uses of...Ch. 2.1 - Prob. 1CYPCh. 2.1 - Prob. 2CYPCh. 2.1 - Prob. 3CYPCh. 2.1 - Prob. 4CYPCh. 2.2 - Prob. 1LOCh. 2.2 - List the different types of bonds that occur...
Ch. 2.2 - Compare the relative strengths of ionic, covalent,...Ch. 2.2 - Identify whether carbon dioxide (CO2) and nitrogen...Ch. 2.2 - Prob. 2CYPCh. 2.2 - Prob. 3CYPCh. 2.3 - Evaluate which properties of water are important...Ch. 2.3 - Identify common acidic and basic substances.Ch. 2.3 - Prob. 3LOCh. 2.3 - Prob. 1QTCCh. 2.3 - Prob. 2QTCCh. 2.3 - Prob. 3QTCCh. 2.3 - Prob. 1CYPCh. 2.3 - Prob. 2CYPCh. 2.3 - Prob. 3CYPCh. 2.4 - Prob. 1LOCh. 2.4 - 2. Identify the role of a functional group.
Ch. 2.4 - Prob. 3LOCh. 2.4 - Prob. 1CYPCh. 2.4 - Prob. 2CYPCh. 2.5 - Prob. 1LOCh. 2.5 - Prob. 2LOCh. 2.5 - Identify the structural element that all...Ch. 2.5 - Prob. 2CYPCh. 2.6 - Compare the structures of fats, phospholipids, and...Ch. 2.6 - Prob. 2LOCh. 2.6 - 1. List the proportion of your plate that should...Ch. 2.6 - Prob. 2QTCCh. 2.6 - Prob. 3QTCCh. 2.6 - Prob. 1CYPCh. 2.6 - Prob. 2CYPCh. 2.7 - Describe the functions of proteins in cells.Ch. 2.7 - 2. Explain how a polypeptide is constructed from...Ch. 2.7 - Compare the four levels of protein structure.Ch. 2.7 - Prob. 1CYPCh. 2.7 - Describe how amino acids are formed.Ch. 2.7 - Compare and contrast the four levels of protein...Ch. 2.8 - Prob. 1LOCh. 2.8 - Prob. 2LOCh. 2.8 - Prob. 1QTCCh. 2.8 - Prob. 2QTCCh. 2.8 - Prob. 3QTCCh. 2.8 - Prob. 1CYPCh. 2.8 - Prob. 2CYPCh. 2 - Prob. S1.1BYBCh. 2 - Prob. F1.2BYBCh. 2 - Prob. S1.3BYBCh. 2 - Prob. 1CSCh. 2 - Prob. 2CSCh. 2 - Prob. 1ACh. 2 - Prob. 2ACh. 2 - Prob. 3ACh. 2 - Prob. 4ACh. 2 - Prob. 5ACh. 2 - Prob. 6ACh. 2 - Prob. 7ACh. 2 - Prob. 8ACh. 2 - Prob. 9ACh. 2 - Prob. 10ACh. 2 - Prob. 11ACh. 2 - Prob. 12ACh. 2 - Prob. 13ACh. 2 - Prob. 14ACh. 2 - Prob. 1TCCh. 2 - Because proteins are composed of the same limited...Ch. 2 - Prob. 3TC
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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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