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BIOL10011 Lecture Notes - Hemoglobin

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30 Jan 2022
School
Mohawk College
Department
BIOL
Course
BIOL10011
Professor

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Document Summary

Studies have discovered the latest technological device used to measure the percentage of haemoglobin in the blood, and this device is very accurate in its results. The eco test device is characterised by its low cost, and anyone can buy it and use it at home without having to go to the testing laboratories, as it is easy to use. Also, this (eco test) device enjoys a warranty for about a full year if it has any manufacturing defects, and the company will replace the device.

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Related Questions

Police find a man unconscious in his car near Marion Shopping Centre. The car engine was running
with a hose taped to the exhaust carrying exhaust gases to the car's interior. The police take the
man to the FMC Emergency department where an arterial blood sample is taken and the man given
oxygen. Lack of oxygen may lead to changes in arterial blood gas results. In this case, carbon
monoxide, which is found in car exhaust, to various extents prevents oxygen from binding to
haemoglobin resulting in tissue hypoxia. Blood gas and co-oximetry measurements (the values of
oxyhemoglobin and carboxyhaemoglobin which show how much oxygen and carbon monoxide is bound to
haemoglobin, respectively) on the pre-treatment arterial blood give the following values:

RESULT UNITS REFERENCE RANGE
PO2 85 mmHg (80-100)
PCO2 30 mmHg (35-45)
HCO3- 18 mmol/L (21-28)
pH 7.31
(7.35-7.45)
Total
Haemoglobin 151 g/L
(130-175)
Oxyhaemoglobin 57%
(94-100%)
Carboxy-
haemoglobin 40%
(<2%, non-smoker)

a) Briefly explain the likely reason for this man’s unconsciousness. (1 mark)
b) Explain why his blood pH is below the normal range. Outline any relevant metabolic events and
indicate why these occur in this situation. (4 marks)
c) suggest explanation for the low PCO2 and HCO3- levels observed,
outlining any relevant mechanism(s). (5 marks)

Question 2

a.) Describe the structure and function of haemoglobin (Hb). You should include a description of both tertiary and quaternary structures of the protein and the location and function of non-protein components.

b.) List the sequence of intra-molecular movements that results in the conformational change of haemoglobin when it binds oxygen.

c.) Explain why binding affinity of carbon monoxide (CO) to haem (heme) is reduced when haem is incorporated into myoglobin or haemoglobin.

2. Identify and discuss the structure of haemoglobin and the red blood cell membrane.