Lecture 16 Flashcards

1
Q

What is the composition of air?

A

Dry and wet at standard atmospheric pressure of 760 mmHg

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2
Q

What is Dalton’s law?

A

The total pressure of a mixture of gases is the sum of their individual partial pressures

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3
Q

What can partial pressure information influence?

A

How much gas we have in a solution

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4
Q

Concentration of a gas dissolved in a solution is determined by…

A

Henry’s law

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5
Q

What is the equation of Henry’s law?

A

Concentration of dissolved gas = Solubility coefficient x Partial pressure of gas

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6
Q

Does plasma carry a lot of oxygen?

A

no

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7
Q

What is the molecular weight of haemoglobin?

A

68 kD

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8
Q

What is the globin chain combination for adult haemoglobin?

A

2 alpha chains and 2 beta chains

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9
Q

What is the globin chain combination for fetal haemoglobin?

A

2 alpha chains and 2 gamma chains

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10
Q

What is a haem unit?

A

Porphyrin ring containing a single iron atom

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11
Q

What enzyme converts Fe (3+) to Fe (2+) in the haem unit?

A

Methaemoglobin reductase

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12
Q

How much of hemoglobin is saturated in arterial blood?

A

98%

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13
Q

What is the effect of temperature on hemoglobin saturation?

A

If temperature increases, curve shifts to the right
- hemoglobin carries less oxygen
If temperature decreases, curve shifts to the left
- hemoglobin carries more oxygen

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14
Q

What is the effect of pH on hemoglobin saturation?

A

pH and CO2 are closely interlinked factors
CO2 (weak acid)
Increase in CO2: acidification - shifts to the right
(less oxygen)
Alkalization - shifts to the left (more oxygen)

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15
Q

What is the name for changes in saturation due to pH changes?

A

Bohr effect

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16
Q

What is the effect of 2,3-Diphosphoglycerate (2,3-DPG)?

A

Interacts with beta-chain and changes the interaction of hemoglobin with oxygen
- an increase in 2,3 DPG concentration shifts curve to the right, decrease shifts to the left
2,3, DPG tends to bind more to hemoglobin in an deoxygenated state
- changes affinity for oxygen so that it aids oxygen offloading

17
Q

What is fetal hemoglobin like?

A

Globin chains are insensitive to 2,3 DPG

Fetal hemoglobin is like adult hemoglobin at 0 concentration of 2,3 DPG

18
Q

What is the advantage to the insensitivity to 2,3 DPG in fetal hemoglobin?

A

Helps fetus scavenge oxygen from mother’s blood more efficiently

19
Q

How does the blood carry CO2 as?

A
Dissolved CO2
Carbonic acid
Bicarbonate (largest component)
Carbonate
Carbamino compounds (CO2 interacts with proteins in the lung)
20
Q

How is bicarbonate efficient as a buffering system?

A

22~25 bicarbonate in plasma
1.2 mM
ph 7.4
helps maintain that pH within tight barriers
Hyperventilating: blowing of CO2 - effect on plasma pH

21
Q

How much of CO2 stays in the plasma?

A

10% stays in plasma

22
Q

How much of CO2 remains dissolved?

A

6%

23
Q

How much of CO2 combines with proteins to form carbamino compounds?

A

less than 1

24
Q

What enzyme speeds up process of bicarbonate formation?

A

Carbonic anhydrase type 2

25
Q

What are channels used for CO2 transport?

A

aquaporin 1, Reces A (50% of transport)

26
Q

What happens when CO2 binds to hemoglobin?

A

Proton formed

  • local acidification in RBC
  • favors oxygen being released from iron group
  • leaves RBC
  • supply to tissues
27
Q

What role does AE 1 (band 3 - anchoring chain) have in bicarbonate transport?

A

Important role in anchoring cytoskeleton (contributes to shape of RBC)

  • Cl moves in and HCO3 out
  • Hamburger shift (Cl shift)
  • all processes are in reverse in lungs - higher affinity to bind to oxygen