Gas Transport Flashcards
Describe how oxygen is transport in the blood?
Physically dissolved in plasma (2%) and combined with haemoglobin (98%)
Describe why only a small amount of blood is physically dissolved in plasma
At 37 degrees, the solubility of oxygen in plasma is poor (0.03) and the partial pressure of oxygen in arterial blood is 100mmHg so only 3ml oxygen per litre of blood can be transported. Much less than our bodies consume.
Describe the structure oh haemoglobin
Tetramer with four O2-binding heme groups. Consists of two alpha and two beta chains. Each heme group consists of a porphyrin ring surrounding an iron ion.
How can oxygen bind to iron
Only in ferrous state
Describe how haemoglobin structure changes with oxygenation
Deoxygenated Hb exists in a tensed state. In this state strong ionic bonds form between the 4 polypeptide chains which means Fe lies deeper in the pocket and cannot bind O2. Where as oxygenated Hb is in a relaxed state, this occurs because when oxygen binds the ionic bonds break so Fe moves to plane of porphyrin ring. Colour of blood changes from dark red to bright red.
What accounts for the shape of the O2-Hb dissociation curve?
Cooperatively (haem-haem interaction). This means that the binding of one O2 molecules makes it easier for subsequent ones to attach
With quite respiration how much oxygen does haemoglobin deposit?
47ml/L of blood. This will increase if undergoing exercise
What is oxygen capacity and what does it depend on?
The amount oxygen/L of blood attached to Hb at full saturation. It depends on Hb concentration in blood
Each gram of Hb can carry how much oxygen?
1.35ml
Describe the effects of myoglobin and foetal haemoglobin?
They shift the curve to the left
What is the difference between adult and foetal haemoglobin
Foetal - 2 alpha and 2 gamma chains. This means foetal haemoglobin has a higher affinity for oxygen than adult due to the special properties of the gamma chains
What causes the haemoglobin oxygen dissociation curve to shift to the left and what does this mean and where does this commonly occur
- Increase in pH, a decrease in PCO2, decrease in temperature and a decrease in 2,3 DPG. This means the haemoglobin has a high affinity for oxygen, this occurs in pulmonary capillaries
What causes the haemoglobin oxygen dissociation curve to shift to the right and what does this mean and where does this commonly occur
- Decrease in pH and an increase in PCO2, temp and 2,3-DPG. This means Hb has a low affinity for oxygen, occurs in systemic capillaries
Describe what factors account for the bohr effect
pH accounts for most of it.
Temperature will affect O2 capacity of Hb.
Hypocapnia as CO2 combines with unprotonated amino group on Hb forming carbamino haemoglobin.
2,3 Diphosphoglycerate - By product of glycolysis, if there is a decrease in PO2, RBCs stimulate glycolysis resulting in increased levels of 2,3 DPG
Describe the effects of carbon monoxide on Hb affinity for oxygen
CO has a 200 fold greater affinity for Hb than oxygen so maximal oxygen capacity falls to the extend that CO binds. However it also increases oxygen affinity of Hb, shifting dissociation curve to the left (meaning Hb doesn’t release oxygen when it gets to tissue).