3.1.2 - Transport In Animals (set C - Transport Of Substances) Flashcards
What are erythrocytes?
Red blood cells - very specialised and have a number of adaptions to their main function of transporting oxygen
Explain how erythrocytes are adapted for their role - give 2 ways and explain them?
- biconcave shape - provides a larger SA then just a simple disk structure, more SA available for diffusion of gases, helps with moving through narrow capillaries
- mature erythrocytes loose their nuclei when they enter circulation - maximises amount of Haemoglobin that fits into cells, as well as limiting their life (about 120 days in bloodstream)
Explain what Haemoglobin is?
Red pigment that carries oxygen (gives erythrocytes their colour) - is a very large globular conjugated protein, made up of four peptide chains, each with an iron-containing haem prophetic group
- oxygen binds loosely to Haemoglobin forming oxyhaemoglobin
Explain what type of protein Haemoglobin is?
Very large globular conjugated protein made up of four peptide chains, each with an iron-containing haem prosthetic group
Give the equation for Haemoglobin binding with oxygen?
Haemoglobin + oxygen - oxyhaemoglobin
Explain the process of oxygen binding to Haemoglobin?
Erythrocytes enter the capillaries in the lungs, the oxygen levels in the cells are relatively low creating a seep concentration gradient between the inside of the erythrocytes and the air in the alveoli - this causes oxygen to move into the erythrocytes and bind with the Haemoglobin
Explain positive cooperativity, and how it takes place?
Arrangement of the Haemoglobin molecule means that as soon as one oxygen molecules binds to a haem group the molecule changes shape - making it easier for the next oxygen molecule to bind
Explain fully the process of erythrocytes receiving oxygen in the lungs?
Erythrocytes enter capillaries in lungs (oxygen levels in cell are low) steep concentration gradient between inside of erythrocytes and air in alveoli
Oxygen moves into the erythrocytes and binds with Haemoglobin - molecule changes shape (positive cooperativity) easier for next oxygen molecule to bind
Diffusion gradient is maintained until all the Haemoglobin is saturated with oxygen
Explain how a seep diffusion gradient is maintained in erythrocytes in the capillaries of lungs?
Because the oxygen is bound to the Haemoglobin, the free oxygen concentration in the erythrocyte stays low, so a steep diffusion gradient is maintained until all of the Haemoglobin is saturated with oxygen
Explain what happens when erythrocytes reaches body tissues?
The concentration of oxygen in the cytoplasms of the body cells is lower than in the erythrocytes - oxygen moves out of the erythrocytes down a concentration gradient - once the first oxygen molecule is released by the Haemoglobin, the molecule changes shape making it easier to remove the remaining oxygen molecules
What is the oxygen dissociation curve?
Graphical representation of the relationship between the percentage saturation Haemoglobin in the blood against the partial pressure of oxygen
Explain why a small change in the pressure of oxygen makes a significant difference to the saturation of Haemoglobin?
once the first molecule becomes attached with a haem group, the change in shape means other oxygen molecules are added rapidly (positive cooperativity)
Describe the oxygen dissociation curve for human Haemoglobin?
1) at low partial pressure of oxygen, few Haem groups are bound to oxygen, so Haemoglobin does not carry much oxygen
2) at higher partial pressure of oxygen, more haem groups are bound to oxygen, so it changes shape and makes it easier for more oxygen to be picked up
3) the Haemoglobin becomes saturated at very high partial pressure of oxygen as all the haem groups become bound - curve levels out, no more oxygen uptake
Explain where the difference in partial pressure of oxygen occurs?
- High partial pressure of oxygen in the lungs, so haemoglobin in the erythrocytes are rapidly loaded with oxygen
- relatively small drop in oxygen levels in the respiring tissues means oxygen is released rapidly from haemoglobin to diffuse into the cells
Explain why partial pressure of oxygen is important?
The partial pressure of oxygen has a significant effect on wether oxygen will bind to, or be released from haemoglobin
Explain the change known as bohrs effect?
As the partial pressure of carbon dioxide rises (higher partial pressure of carbon dioxide), Haemoglobin gives up oxygen more easily - the Bohrs effect is important in the body
Explain 2 ways bohrs effect is important in the body?
- in active tissues with a high partial pressure of carbon dioxide, haeomoglobin gives up oxygen more readily
- in the lungs where the proportion of carbon dioxide in the air is relatively low, oxygen binds to the haemoglobin molecules easily
Explain fetal haemoglobin?
When a fetus is developing it’s completely dependent on the mother to supply it with oxygen - oxygenated blood from the mother runs close to the deoxygenated fetus blood in the placenta - oxygen removed from maternal blood due to fetal blood having higher affinity for oxygen
Explain the problem if the blood of the fetus had the same affinity for oxygen as the mother?
if the blood of the fetus had the same affinity for oxygen as the blood of the mother, then little to no oxygen would be transferred to the blood of the fetus
Explain the problem between the mother and fetal blood, explain how its avoided?
If the affinity for oxygen is the same for both bloods, then none would need transferred to the blood of the fetus
Fetal haemoglobin has a higher affinity for oxygen than adult haemoglobin - so it removes oxygen from the maternal blood as they move past each other