Blood💋 Flashcards
What is heamoglibin?and function?
-are a group of chemically stable molecules found in most organisms
With a quaternary structure evolved to make it effective at loading and unloading oxygen based on condition
Describe the structure of heamoglibin
Each 4 polypeptide chain is associated with a beam group with a ferrous ion (Fe2+) and each the ions combine with oxygen molecule (total of 4 oxygen molecules can be carried) by 1 haemoglobin.
What is loading or associating and unloading dissociation ?
Loading is haemoglobin binds to oxygen taking place in the lungs
Unloading is haemoglobin releases oxygen taking place in tissues
What is the binding of oxygen to haemoglobin and unbinding?
-oxyhemoglobin
-deoxyhemoglobin
What is the adaptation for haemoglobin to do its function?
-readily associate with oxygen where gas exchange occurs
-readily dissociate with oxygen when respiring tissues
What is the affinity?what much haemoglobin has to change to dissociate and associate with oxygen?
-It is the chemical attraction between molecules
-haemoglobin has to change its affinity for oxygen depending on the conditions present.
➔Just like other proteins, it changes shape based on conditions:
◆ E.g - At respiring tissues = high CO2 concentration → haemoglobin
has a lower affinity to O2 = oxygen dissociates.
Many organisms possess haemoglobin.
However, each species produces a slightly different amino acid sequence.
What effect will this have on the haemoglobin protein?
Each species has a slightly different final protein structure changing the proteins affinity to oxygen.
E.g squid and octopuses it is blue called haemocyanin
Explain to me what happens in the gas exchange surface?(in lungs)
There is a high concentration of oxygen and low of carbon dioxide and the heamoglibin affinity to oxygen is high and oxygen associates
Explain to me what happens when tissue are respiring?
There is a low concentration of oxygen and high of carbon dioxide and haemoglobin affinity to oxygen is low and oxygen is disassociated
