1- Gas transport in the blood part 1 Flashcards

1
Q

what is effect of partial pressure on gas solubility?

A

according to henry’s law the amount of given gas dissolved is proportional to partial pressure of gas in equilibrium with liquid

= this means that if partial pressure of gas is increased then concentration of gas in the liquid (e.g. blood) is increased proportionally

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2
Q

how many ml of oxygen is dissolved per litre of blood?

A

3ml O2 per litre at partial pressure oxygen 13.3 kPa (100 mmHg)

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3
Q

how much oxygen is taken to tissues as dissolved oxygen under
a) resting conditions
b) strenuous exercise

A

a) (cardiac output 5L/min): 15 ml/min
b) (cardiac output of 30 L/min): 90 ml/min

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4
Q

what is most oxygen in blood transported by?

A

by being bound to haemoglobin in red blood cells = 98.5 %
- only 1.5% carried in dissolved form

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5
Q

how much oxygen is bound to haemoglobin?

A

haemoglobin molecule = 4 haem groups which each reversible bind to 1 O2 molecule
fully saturated = 4 O2

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6
Q

what is the primary factor that determines the percent saturation of haemoglobin with O2?

A

oxygen partial pressure

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7
Q

what is structure of haemoglobin?

A

4 haem groups with beta and alpha chains (2 of each)

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8
Q

what is the relationship described by oxygen haemoglobin dissociation curve?

A

oxygen partial pressure increases as more haemoglobin bound =sigmoidal shape

  • this indicates co-operactivity (more bound means more attractive for other O2 to come and bind)

*so saturation of haemoglobin dependant on partial pressure of oxygen (as also works opposite way, not much oxygen means less attractive for oxygen to go and bind)

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9
Q

how do you calculate oxygen content of arterial blood (CaO2)?

A

1.34 x concentration of haemoglobin x %Hb saturated with oxygen (determined by oxygen partial pressure)

*1g of Hb carry 1.34 ml O2 when fully saturated

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10
Q

when can oxygen delivery to tissues be impaired?

A

respiratory disease & decreased partial pressure of inspired oxygen = decrease arterial PO2 & hence decrease Hb saturation with O2 & O2 content in blood

heart failure = decreases CO

anaemia = decreases Hb hence decreases O2 content in blood

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11
Q

what does partial pressure of inspired oxygen depend on?

A

atmospheric pressure (total pressure) and proportion of oxygen in gas mixture (about 21% in atmosphere)

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12
Q

explain how the sigmoidal oxygen haemoglobin dissociation curve shows co-operactivity?

A

flat upper portions = moderate fall in alveolar PO2 but not enough to affect loading of haemoglobin (not enough people at party to make attractive)
steep lowering = crosses threshold at about 8 kPa where enough oxygen there and now bind so everyone wants to go and bind

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13
Q

what is the bohr effect?

A

phenomenon where Hb saturation decreases as the following increase:
- partial pressure of CO2
- concentration of H+ (acidity)
- temperature
- 2,3-biphosphoglycerate

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14
Q

what is different about fetal haemoglobin?

A
  • differs in structure - 2 alpha and 2 gamma (instead of 2 alpha and 2 beta)
  • hence interacts less with 2,3 - bisphosphoglycerate in RBC’s
  • therefore have higher affinity for oxygen compared to adult haemoglobin means dissociation curve for HbF is shifted to left comparte to HbA
  • means more saturation

*doesn’t have sigmoidal curve and not same co-operactivity so allows O2 to transfer from mother to foetus even if PO2 low

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15
Q

where is myoglobin found?

A

skeletal & cardiac muscle not blood

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16
Q

what is different about myoglobin and haemoglobin structure?

A
  • only 1 haem group per molecule so no cooperative binding of O2
  • dissociation curve hyperbolic not sigmoid
  • myoglobin releases O2 at very low PO2
    (short term storage of O2 for anaerobic conditions)
17
Q

what does presence of myoglobin in blood mean?

A

muscle damage

18
Q

what contributes to off loading of O2 at tissues?

A

bohr effect = less saturation when high metabolism (acidic), high temperature, high carbon dioxide partial pressure and high 2,3-biphosphoglycerate

= this means oxygen unloaded at cells that are metabolising and also myoglobin at muscle cells (have higher affinity for O2)