Heamoglobin Flashcards
Describe how haemoglobin normally loads oxygen in the lungs and unloads it in a tissue cell.
Oxygen combines (reversibly) to produce oxyhaemoglobin;
• each haemoglobin molecule/ one haemoglobin may transport 4 molecules of oxygen;
• high partial pressure of oxygen / oxygen tension / concentration in lungs;
• haemoglobin (almost) 95% / 100% saturated;
• unloads at low oxygen tension(in tissues);
• presence of carbon dioxide displaces curve further to right / increases oxygen dissociation;
• allows more O2 to be unloaded;
• increase temp/ acidity allows more O2 to be unloaded;
• low pO2 / increase CO2 / increase term / increase acid occur in vicinity of respiring tissue;
Explain how oxygen in a red blood cell is made available for respiration in active tissues.
• CO2 (increased) respiration;
• (increased) dissociation oxygen from haemoglobin;
• Low partial pressure in tissues/plasma;
• Oxygen diffuses from r.b.c. to tissues;
The oxygen dissociation curve of the foetus is to the left of that for its mother. Explain the advantage of this for the foetus.
Higher affinity / loads more oxygen;
• At low/same/high partial pressure/pO2;
• Oxygen moves from mother/to fetus;
Explain how oxygen is loaded, transported and unloaded in the blood. (6)
• Haemoglobin carries oxygen / has a high affinity for oxygen / oxyhaemoglobin;
• In red blood cells;
• Loading/uptake/association in lungs at high p.O2;
• Unloads/ dissociates / releases to respiring cells/tissues at low p.O2;
• Unloading linked to higher carbon dioxide (concentration);
Binding of one molecule of oxygen to haemoglobin makes it easier for a second oxygen molecule to bind.
- Binding of first oxygen changes tertiary / quaternary (structure) of haemoglobin; [conformational shift caused]
- Creates / leads to / uncovers second / another binding site OR Uncovers another iron / Fe / haem group to bind to;
Describe and explain the effect of increasing carbon dioxide concentration on the dissociation of oxyhaemoglobin.
- Increases/more oxygen dissociation/unloading OR Deceases haemoglobin’s affinity for O2;
- (By) decreasing (blood) pH/increasing acidity;
Describe and explain the effect of increasing carbon dioxide concentration on the dissociation of oxyhemoglobin.
- Increases dissociation of oxygen;
Accept unloading/ release/reduced affinity for
dissociation
For aerobic respiration at the tissues/muscles/cells
OR
Anaerobic respiration delayed at the tissues/muscles/cells
OR
Less lactate at the tissues/muscles/cells;
Give the formula when calculating percentage of saturation of haemoglobin with oxygen:
Oxygenated Hb
—————————- X100
Maximum saturation
Define partial pressure of oxygen (pO2/kPa)
The amount of oxygen in a mixture of gases or a solution
LOWER pO2 means…
LESS Hb is saturated
Lower pO2 in…
Tissues when at rest
Higher PO2 in…
Lungs (high saturation of Hb)
pO2 in lungs:
Hb has a higher affinity for O2 at high pO2
Hb becomes fully saturated
pO2 in respiring tissues:
Hb lower affinity for O2 at lower pO2
So oxyhaemoglobin starts to unload oxygen
To be used in aerobic respiration
What is the effect of increase respiration on oxygen dissociation?
- Tissue cells respirier aerobically reducing dissolved O2 in surrounding tissue fluid
- Reduces the O2 to a lower level than normal
- Oxygenated blood arriving with fully saturated Hb unloads MORE oxygen and MORE oxygen will be released from Hb to the tissue cells
- Because surrounding pO2 is lower so Hb has an even lower affinity to oxygen