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Systems 1 Part 2 > Blood Gas Transport > Flashcards

Blood Gas Transport Flashcards

1
Q

common measure of oxygenation

A

Alveolar to arterial oxygen gradient (A-a)

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2
Q

How do you measure PaO2?

A

arterial blood gas

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3
Q

How do you calculate PAO2?

A

alveolar gas equation

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4
Q

FiO2

A

fraction of inspired O2

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5
Q

what is FiO2 in room air?

A

0.21

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6
Q

what is atm P at sea level

A

760 mmHg

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7
Q

what is the partial P of water

A

47 mmHg

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8
Q

what is PaCO2?

A

arterial CO2 tension

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9
Q

the A-a gradient calculated may deviate from the true gradient by up to –

A

10 mmHg

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10
Q

the normal A-a gradient varies with –

A

age

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11
Q

A-a gradient increases with –

A

higher FiO2

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12
Q

How does A-a gradient increase with high FiO2?

A

both PAO2 and PaO2 increases but PAO2 increases disproportionately

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13
Q

The use of a 100 percent non-rebreathing mask reasonably approximates actual – and can be used to measure shunt.

A

delivery of 100 percent oxygen

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14
Q

normal PaCO2

A

40

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15
Q

normal PaO2

A

100

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16
Q

Henry’s lawstates that at a constant temperature, the amount of a gas that is dissolved in a liquid is directly proportional to –

A

the partial pressure of that gas

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17
Q

This law provides the explanation for decompression sickness and nitrogen narcosis.

A

Henry’s law

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18
Q

Henry’s law directly – the amount of gas that can be dissolved in plasma.

A

limits

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19
Q

Hemoglobin is an –

A

iron-porphyrin compound

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20
Q

each globin chain has a –

A

heme moeity

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21
Q

amount of hemoglobin in an adult male

A

[Hb] = 15 g/dL

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22
Q

how much oxygen can Hb carry

A

200 ml/L

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23
Q

Different types of heme have different – and disorders of hemoglobin affect the ability to carry oxygen

A

oxygen affinity

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24
Q

which type of iron doesn’t bind oxygen that well

A

ferric (Fe3+)

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25
Q

Hemoglobin undergoes a conformational change when –

A

oxygenated

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26
Q

Hb conformational change leads to – in pulse oximetry

A

color change

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27
Q

hemoglobin/oxygen binding curve, we see a steep slope up to a –, then starts to flatten

A

PO2 of about 50

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28
Q

Note that beyond a –, the hemoglobin binding of oxygen barely increases at all

A

PO2 of 100

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29
Q

Oxygen saturation is determined by the percentage of –

A

available Heme binding sites that have bound oxygen

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30
Q

In normal conditions, a PO2 of 100 gives SpO2 (oxygen saturation) of about –.

A

97.5%

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31
Q

A shift to the right in the hemoglobin-oxygenassociation/dissociationcurve indicates that a – partial pressure of oxygen is required to saturate hemoglobin at the level of the lungs

A

larger

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32
Q

a right shift in the hemoglobin-oxygenassociation/dissociationcurve, corresponds to – affinity

A

reduced oxygen

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33
Q

potent modulator of the affinity of hemoglobin for oxygen

A

2,3 bisphosphoglycerate

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34
Q

2,3-BPG is a polyanion that binds strongly to –

A

deoxyhemoglobin

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35
Q

2,3-BPG is a polyanion that binds weakly to

A

oxyhemoglobin

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36
Q

Binding takes place in the – where the negative charges of 2,3-BPG are neutralized by the beta NH2 terminus histidine, beta82 lysine, and beta143 histidine.

A

central cavity between the two beta chains

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37
Q

Binding to – helps to stabilize the tense (T) structure of hemoglobin and decrease oxygen affinity.

A

deoxyhemoglobin

38
Q

In oxyhemoglobin, the – are insufficiently spread apart to permit firm binding of 2,3-BPG.

A

H helices of the beta chains

39
Q

Increasing levels of 2,3-BPG – oxygen affinity

A

decrease

40
Q

Increasing levels of 2,3-BPG shift the hemoglobin oxygen dissociation curve to the –

A

right

41
Q

Increasing levels of 2,3-BPG – the delivery of oxygen to tissues

A

increase

42
Q

Decreased levels of 2,3-BPG due to a BPGM mutation lead to a – shift in the hemoglobin oxygen dissociation curve

A

left

43
Q

Decreased levels of 2,3-BPG leads to a – delivery of oxygen to tissues.

A

decreased

44
Q

Decreased delivery of oxygen to tissue leads to increased production of –

A

erythropoietin

45
Q

Oxygen affinity varies – with temperature

A

inversely

46
Q

CO2can react with free amino groups at the N termini of the alpha and beta chains to form –

A

carbamino complexes

47
Q

carbamino complexes is formed more readily by –

A

deoxyhemoglobin

48
Q

at any given pH, CO2 – oxygen affinity

A

lowers

49
Q

Normally, approximately 10 percent of CO2is – in the form of carbamino hemoglobin

A

transported to the lungs

50
Q

The oxygen affinity of hemoglobin increases as a function of pH over a range of –, a phenomenon known as the Bohr effect.

A

6.0 to 8.5

51
Q

Under physiologic conditions, a molecule of hemoglobin releases approximately – upon oxygenation.

A

2.8 protons

52
Q

A substantial portion of the Bohr effect is due to an – between the positively charged imidazole of beta146 histidine and the negatively charged carboxyl of beta94 aspartate

A

intrasubunit salt bond

53
Q

Molecular changes when Hb is oxygenated?

A

salt bond breaks and protons are released

54
Q

two main physiological consequences of Bohr Effect

A

more oxygen is delivered to tissues and oxygen is more easily taken up in pulmonary circulation

55
Q

how is CO2 carried in blood?

A

dissolved gas, bicarbonate ions, carbamino compounds

56
Q

solubility CO2 in plasma

A

0.67 ml/L/mmHg

57
Q

solubility O2 in plasma

A

0.03 ml/L/mmHg

58
Q

what makes up the bulk of CO2 transport

A

bicarbonate ions

59
Q

CO2 dissociates in water to –

A

carbonic acid

60
Q

the dissociation of CO2 into water and carbonic acid is – in plasma

A

slow

61
Q

the dissociation of CO2 into water and carbonic acid is accelerated in the cell by –

A

carbonic anhydrase

62
Q

dissociation of carbonic acid into – happens quickly

A

bicarbonate and hydrogen ions

63
Q

– shifts into the cell from the plasma to maintain electrical neutrality

A

Chloride

64
Q

– shifts easily out of the cell

A

bicarbonate

65
Q

hydrogen ions diffuse more slowly due to the – of the cell membrane to cations

A

relative impermability

66
Q

since deoxy Hb is – it can readily bind the protons of the dissociated hydrogen ions

A

reduced (proton acceptor)

67
Q

higher dissolved CO2 proportion in –

A

venous

68
Q

higher bicarbonate proportion in –

A

arterial

69
Q

higher carboamino proportion in –

A

venous

70
Q

CO2 dissociation curve is much more – than oxygen curve

A

linear and steeper

71
Q

the difference between the arterial and venous CO2 dissociation curves is explained –

A

Haldane effect

72
Q

Haldane effect

A

oxygen unloading increases CO2 affinity

73
Q

T/F: CO forms stable bonds with heme moiety

A

true

74
Q

compared to oxygen, CO has a – affinity to Hb

A

higher (200x)

75
Q

In general, a – difference in arterial and venous oxygen content per 100 mL blood is expected at rest.

A

5 mL

76
Q

the effect of a 50% decrease in Hb (anemia) decreases – but does not change the partial pressure at which Hb is 50% saturated (same P50)

A

A’ (arterial) and venous oxygen content

77
Q

bind more CO2 on – side (deoxygenated) than arterial

A

venous

78
Q

CO2 dissociation curve is – than the O2 dissociation curve

A

steeper

79
Q

CO will shift O2 dissociation curve to the –

A

left

80
Q

anemia = lower Hb decreases O2 content but not –

A

oxygen saturation

81
Q

effect of carboxyhemoglobinema (COHb)

A

decreases oxygen carrying capacity and impairs peripheral unloading of O2 at low oxygen tension

82
Q

methemoglobinemia occurs when Fe2+ in heme are – to ferric fe3+

A

oxidized

83
Q

methemoglobinemia unable to –

A

reversibly bind oxygen

84
Q

methemoglobinemia – shift oxygen dissociation curve

A

left

85
Q

methemoglobinemia has higher incidence in – due to medication toxic effects

A

G6-PD deficiency

86
Q

methemoglobinemia creates less functional Hb and impairs –

A

delivery of oxygen to tissues

87
Q

clinical clues of methemoglobinemia

A

sudden cyanosis with hypoxia, hypoxia doesn’t improve with O2, dark red muddy brown blood

88
Q

does methemoglobinemia blood change color like deoxyHb when exposed to oxygen?

A

no

89
Q

T/F: methemoglobinemia has a normal arterial PO2 (PaO2)?

A

true

90
Q

methemoglobinemia can be caused by –

A

topical local anesthetics

91
Q

can cyanide poisoning resolve with time?

A

no

92
Q

what causes a left shift in the Hb-O2 dissociation curve?

A

decreased temp, decreased 2,3-BPG, decreased [H+], increased pH, CO

Systems 1 Part 2 (27 decks)

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