4- transport of gases in blood Flashcards

(12 cards)

1
Q

structure of haemoglobin

A
  • composed of four polypeptide chains: two alpha chains and two beta chains
  • each chain has a haem group with an iron atom, which can bind to one molecule of oxygen
  • one haemoglobin molecule can carry up to four oxygen molecules
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2
Q

role of haemoglobin in gas exchange

A
  • haemoglobin transports O2 from the lungs to tissues and CO2 from tissues to the lungs
  • oxygen transport: oxygen binds to the iron in the haem groups, forming oxyhaemoglobin
  • carbon dioxide transport: some carbon dioxide is carried in the bloodstream bound to haemoglobin (carbaminohaemoglobin)
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3
Q

Bohr affect on haemoglobin

A
  • the effect of pH on the oxygen- binding affinity of haemoglobin
  • high pH (low carbon dioxide concentration): leads to a higher affinity for oxygen, facilitating oxygen uptake in the lungs
  • low pH (high carbon dioxide concentration): leads to a lower affinity for oxygen, facilitating oxygen release in respiring tissues
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4
Q

oxygen dissociation curve

A
  • a graph showing the relationship between oxygen pressure (PO2) and the oxygen- carrying capacity of haemoglobin
  • sigmoidal shape: indicates that as the oxygen pressure increases, more oxygen binds to haemoglobin until it becomes fully saturated
  • left shift: occurs at higher pH levels, lower temperatures, or lower carbon dioxide levels- this signifies a higher affinity of haemoglobin for oxygen
  • right shift (bohr effect): occurs at lower pH levels, higher temperature, or higher carbon dioxide levels, this signifies a lower affinity of haemoglobin for oxygen
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5
Q

myoglobin structure

A
  • single polypeptide chain with 153 amino acids
  • contain one heme (iron containing) group
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6
Q

function of myoglobin

A
  • stores oxygen in muscle cells, releasing it during periods of hypoxia or intense exercise
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7
Q

myoglobin vs haemoglobin

A
  • haemoglobin is a tetramer, with four polypeptide subunits. myoglobin is monomeric
  • haemoglobin transports oxygen in the blood from the lungs to the tissues. myoglobin stores oxygen in muscle cells
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8
Q

myoglobin oxygen affinity

A

myoglobin has higher oxygen affinity than adult haemoglobin, to store oxygen effectively

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9
Q

structure of foetal haemoglobin

A
  • composed of two alpha and two gamma chains
  • contains two heme groups
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10
Q

function of foetal haemoglobin

A

transports oxygen from mothers bloodstream to the foetus

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11
Q

foetal haemoglobin vs adult haemoglobin

A
  • adult haemoglobin is made up of two alpha and two beta chains. foetal haemoglobin has two alpha and two gamma chains
  • foetal haemoglobin has a higher oxygen affinity than adult haemoglobin, facilitating effective oxygen transfer from mother to foetus
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12
Q

oxygen affinity in foetal haemoglobin

A

higher than adult haemoglobin, to effectively extract oxygen from the mothers blood

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