Introduction To Genetic Analysis
12th Edition
ISBN: 9781319114787
Author: Anthony J.F. Griffiths, John Doebley, Catherine Peichel, David A. Wassarman
Publisher: W. H. Freeman
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Chapter 4, Problem 13P
Summary Introduction
To determine: The approximate location of the wooly locus.
Introduction: Recombination-based techniques can be used to map the positions of centromeres.
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Chapter 4 Solutions
Introduction To Genetic Analysis
Ch. 4 - Prob. 1PCh. 4 - Prob. 2PCh. 4 - Prob. 3PCh. 4 - Prob. 4PCh. 4 - Prob. 5PCh. 4 - Prob. 6PCh. 4 - Prob. 7PCh. 4 - Prob. 8PCh. 4 - Prob. 9PCh. 4 - Prob. 10P
Ch. 4 - Prob. 11PCh. 4 - Prob. 12PCh. 4 - Prob. 13PCh. 4 - Prob. 14PCh. 4 - Prob. 15PCh. 4 - Prob. 16PCh. 4 - Prob. 20PCh. 4 - Prob. 21PCh. 4 - Prob. 22PCh. 4 - Prob. 23PCh. 4 - Prob. 24PCh. 4 - Prob. 25PCh. 4 - Prob. 26PCh. 4 - Prob. 27PCh. 4 - Prob. 28PCh. 4 - Prob. 29PCh. 4 - Prob. 30PCh. 4 - Prob. 30.1PCh. 4 - Prob. 30.2PCh. 4 - Prob. 30.3PCh. 4 - Prob. 30.4PCh. 4 - Prob. 30.5PCh. 4 - Prob. 30.6PCh. 4 - Prob. 30.7PCh. 4 - Prob. 30.8PCh. 4 - Prob. 30.9PCh. 4 - Prob. 30.10PCh. 4 - Prob. 30.11PCh. 4 - Prob. 30.12PCh. 4 - Prob. 30.13PCh. 4 - Prob. 30.14PCh. 4 - Prob. 30.15PCh. 4 - Prob. 30.16PCh. 4 - Prob. 30.17PCh. 4 - Prob. 30.18PCh. 4 - Prob. 30.19PCh. 4 - Prob. 30.20PCh. 4 - Prob. 30.21PCh. 4 - Prob. 30.22PCh. 4 - Prob. 30.23PCh. 4 - Prob. 30.24PCh. 4 - Prob. 30.25PCh. 4 - Prob. 30.26PCh. 4 - Prob. 31PCh. 4 - Prob. 32PCh. 4 - Prob. 33PCh. 4 - Prob. 34PCh. 4 - Prob. 35PCh. 4 - Prob. 36PCh. 4 - Prob. 37PCh. 4 - Prob. 38PCh. 4 - Prob. 39PCh. 4 - Prob. 40PCh. 4 - Prob. 41PCh. 4 - Prob. 42PCh. 4 - Prob. 43PCh. 4 - Prob. 44PCh. 4 - Prob. 45PCh. 4 - Prob. 46PCh. 4 - Prob. 47PCh. 4 - Prob. 47.1PCh. 4 - Prob. 47.2PCh. 4 - Prob. 47.3PCh. 4 - Prob. 47.4PCh. 4 - Prob. 47.5PCh. 4 - Prob. 47.6PCh. 4 - Prob. 47.7PCh. 4 - Prob. 47.8PCh. 4 - Prob. 47.9PCh. 4 - Prob. 47.10PCh. 4 - Prob. 47.11PCh. 4 - Prob. 47.12PCh. 4 - Prob. 47.13PCh. 4 - Prob. 47.14PCh. 4 - Prob. 47.15PCh. 4 - Prob. 47.16PCh. 4 - Prob. 47.17PCh. 4 - Prob. 47.18PCh. 4 - Prob. 47.19PCh. 4 - Prob. 47.20PCh. 4 - Prob. 47.21PCh. 4 - Prob. 47.22PCh. 4 - Prob. 47.23PCh. 4 - Prob. 47.24PCh. 4 - Prob. 48PCh. 4 - Prob. 49PCh. 4 - Prob. 50PCh. 4 - Prob. 51PCh. 4 - Prob. 52PCh. 4 - Prob. 53PCh. 4 - Prob. 54PCh. 4 - Prob. 55PCh. 4 - Prob. 56PCh. 4 - Prob. 57PCh. 4 - Prob. 58PCh. 4 - Prob. 59PCh. 4 - Prob. 60PCh. 4 - Prob. 61PCh. 4 - Prob. 62PCh. 4 - Prob. 63PCh. 4 - Prob. 64PCh. 4 - Prob. 65PCh. 4 - Prob. 66PCh. 4 - Prob. 67PCh. 4 - Prob. 68PCh. 4 - Prob. 69PCh. 4 - Prob. 71PCh. 4 - Prob. 72PCh. 4 - Prob. 73PCh. 4 - Prob. 74PCh. 4 - Prob. 75PCh. 4 - Prob. 76PCh. 4 - Prob. 77PCh. 4 - Prob. 78PCh. 4 - Prob. 79PCh. 4 - Prob. 1GS
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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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