BROOKER BIO 3-HOLE PUNCH W/CONNECT BUND
BROOKER BIO 3-HOLE PUNCH W/CONNECT BUND
5th Edition
ISBN: 9781264065615
Author: BROOKER
Publisher: MCGRAW-HILL LEARNING SOLN.(CC)
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Chapter 10.2, Problem 2CC
Summary Introduction

To determine: The result to be expected if a rat was fed lanthanum and then a sample of a cell layer in the digestive tract was observed under an electron microscope.

Introduction: In a multicellular organism, cells are linked to each other by specialized structures called cell junctions. Three types of junctions are found between cells in animals namely anchoring junctions, tight junctions and gap junctions.

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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
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