Haemoglobin Flashcards

1
Q

Role

A
  • found in RBC

- carry oxygen around the body

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2
Q

Hb

A
  • large protein with a quaternary structure
  • 4 polypeptide chains
  • each chain has a haem group which contains an iron ion and gives Hb its red colour
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3
Q

Oxyhaemoglobin

A
  • oxygen joins to Hb in RBC to form
  • reversible reaction
  • near body cells oxygen leaves oxyHb and returns back to just being Hb
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4
Q

Process Of Joining

A
  • oxygen joining to Hb = association or loading
  • oxygen leaves OxyHb = dissociation or unloading
  • Hb + 402 reversible arrow HbO8
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5
Q

Affinity for oxygen and partial pressure of oxygen

A
  • Hb affinity depends on conditions its in like pO2
  • pO2 measure of oxygen concentration the greater the concentration of dissolved oxygen in cells the higher the partial pressure
  • so as pO2 increases Hb affinity also increases so oxygen loads onto Hb to form OxyHb where there’s high pO2
  • OxyHb unloads its oxygen where there’s a lower pO2
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6
Q

Affinity

A

-tendency a molecule has to bind with oxygen

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7
Q

High pO2

A

-oxygen enters blood capillaries at alveoli where there’s a high pO2 so it loads

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8
Q

Low pO2

A

-when cells respire they use up oxygen so there’s a lower pO2 so RBC deliver oxyhb to respiring tissues where the oxygen is unloaded the hb then returns to lungs to pick up more O2

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9
Q

Alveoli

A
  • high O2 conc
  • high pO2
  • high affinity
  • oxygen loads
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10
Q

Respiring Tissue

A
  • low O2 conc
  • low pO2
  • low affinity
  • O2 unloads
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11
Q

Dissociation curves

A
  • shows how saturated the Hb is with O2 at any given pO2
  • affinity of hb for O2 affects how saturated Hb is
  • where pO2 high hb has high affinity for O2 so high saturation for oxygen
  • low pO2 hb has low affinity for O2 so low saturation of O2
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12
Q

Saturation

A
  • when hb combines with first oxygen its shape alters in a way that makes it easier for other oxygen molecules to join too
  • hb starts to become more saturated which makes it harder for the more oxygen to join
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13
Q

carbon dioxide concentration

A
  • pCO2 affects oxygen unloading

- hb gives up its oxygen more readily at higher pCO2 as its a way of getting more oxygen to cells during activity

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14
Q

Bohr Effect

A
  • when cells respire they produce CO2 which raises pCO2 increasing the rate of oxygen unloading so the dissociation curve shifts to the right
  • saturation of blood lower for given pCO2 as more oxygen is being released so its called bohr effect
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15
Q

Low oxygen environments

A
  • hb with higher affinity for oxygen then human hb
  • isn’t much oxygen available so hb needs to be good at loading any available oxygen
  • curve shifts left
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16
Q

high activity levels

A
  • very active and high oxygen demands have hb with lower affinity for oxygen than human hb
  • need hb top easily unload oxygen
  • curve to right
17
Q

size

A
  • smaller mammals tend to have a higher SA to volume ratio than larger mammals
  • so lose heat quickly
  • high metabolic rate to help them keep warm
  • high oxygen demand
  • mammals smaller than humans have hb with lower affinity for oxygen so they need hb to easily unload oxygen to meet their high oxygen demand
  • curve shifts to the right