MICROBIOLOGY: EVOLV.SCI.-W/ACCESS>CI<
4th Edition
ISBN: 9780393622805
Author: SLONCZEWSKI
Publisher: Norton custom
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Chapter 28.2, Problem 3TQ
Summary Introduction
To review:
The prevention of false positives in ELISA by means of albumin or powdered milk.
Introduction:
Enzyme-linked immunosorbent assay (ELISA) is a type of immunological technique which is used for the detection of antigens as well as antibodies. It is done in 96 well plate which allows testing multiple patient samples at a time. ELISA is classified into four forms namely, direct ELISA, indirect ELISA, sandwich ELISA, and competitive ELISA based on the procedure involved.
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Chapter 28 Solutions
MICROBIOLOGY: EVOLV.SCI.-W/ACCESS>CI<
Ch. 28.1 - Prob. 1TQCh. 28.1 - Prob. 2TQCh. 28.2 - Prob. 1TQCh. 28.2 - Prob. 2TQCh. 28.2 - Prob. 3TQCh. 28.2 - Prob. 4TQCh. 28.2 - Prob. 5TQCh. 28.3 - Prob. 1TQCh. 28.3 - Prob. 2TQCh. 28.4 - Prob. 1TQ
Ch. 28 - Prob. 1RQCh. 28 - Prob. 2RQCh. 28 - Prob. 3RQCh. 28 - Prob. 4RQCh. 28 - Prob. 5RQCh. 28 - Prob. 6RQCh. 28 - Prob. 7RQCh. 28 - Prob. 8RQCh. 28 - Prob. 9RQCh. 28 - Prob. 10RQCh. 28 - Prob. 11RQCh. 28 - Prob. 12RQCh. 28 - Prob. 13RQCh. 28 - Prob. 14RQCh. 28 - Prob. 15RQCh. 28 - Prob. 16RQCh. 28 - Prob. 17RQCh. 28 - Prob. 1TQCh. 28 - Prob. 2TQCh. 28 - Prob. 3TQCh. 28 - Prob. 4TQCh. 28 - Prob. 5TQ
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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.arrow_forwardWith 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_forwardWith 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_forward
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