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HL Bio > D6 gas transport > Flashcards

D6 gas transport Flashcards

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Biology 101 flashcards
1
Q

identify pneumocytes, capillary endothelium cells and blood cells in this light micrograph

A

-

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2
Q

identify a pneumocyte, capillary enodthelium cell and red blood cells in this electron micrograph

A

-

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3
Q

oxygen dissociation curves show the relationship between… (hint: refer to the x and y axes)

A

the partial pressure of oxygen and haemoglobin’s affinity to oxygen

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4
Q

at different partial pressures of oxygen, haemoglobin’s affinity to oxygen _________

A

changes

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5
Q

what is partial pressure? (understanding)

A

the pressure exerted by a gas in a mixture of gases

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6
Q

what’s the concept of cooperative binding (understanding)

A

the more oxygen bound to haemoglobin, the more higher the O2 affinity of haemoglobin

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7
Q

where does the haemoglobin become saturated with O2?

A

at O2 rich areas

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8
Q

at O2 rich areas, % O2 saturation of haemoglobin is [low/high]

A

high

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9
Q

at O2 deficient areas, % O2 saturation of haemoglobin is [low/high]

A

low

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10
Q

oxygen _____ from haemoglobin at O2 deficient areas

A

dissociates

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11
Q

the shape of the oxygen dissociation curve is _____-shaped

A

S

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12
Q

what are the factors that affect haemoglobin’s oxygen affinity?

A
  1. partial pressures
  2. temp
  3. pH
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13
Q

adult haemoglobin has [higher/lower] oxygen affinity than fetal haemoglobin at the same partial pressure

A

lower

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14
Q

why does fetal haemoglobin have higher oxygen affinity than adult haemoglobin at the same partial pressure

A

to ensure that maternal oxyhaemoglobin dissociates to release O2 for binding to fetal haemoglobin

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15
Q

where is myoglobin formed

A

muscle cells

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16
Q

what protein in the muscle cells stores oxygen?

A

myoglobin

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17
Q

what is the function of myoglobin?

A

it stores oxygen

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18
Q

myoglobin has [lower/higher] oxygen affinity than haemoglobin at the same partial pressure

A

higher

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19
Q

how does myoglobin function as an oxygen-storing molecule?

A
  • it has a high affinity for O2
  • it is saturated with oxygen at low partial pressures of O2
  • it only releases oxygen rapidly at very low partial pressures of O2
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20
Q

what type of curve is the oxygen dissociation curve for myoglobin?

A

logarithmic

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21
Q

what is the function of myoglobin in intense exercise?

A
  • during intense exercise, when O2 levels drop
  • it releases O2 stores
  • the slow release delays anaerobic respiration in muscles and lactic acid formation
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22
Q

how is CO2 transported in blood? (3)

A
  • as dissolved CO2 in plasma
  • as hydrogen carbonate ions in plasma
  • bound to haemoglobin as carbaminohaemoglobin
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23
Q

when CO2 binds to haemoglobin it forms…

A

carboaminohaemoglobin

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24
Q

what is the enzyme involved in converting CO2 to HCO3-?

A

carbonic anhydrase

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25
Q

CO2 is converted by carbonic anhydrase into…

A

H+ and HCO3- (aka carbonic acid)

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26
Q

where is carbonic anhydrase found in?

A

RBC

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27
Q

where is HCO3- found in?

A

blood plasma

28
Q

what ion causes blood to become more acidic?

A

H+

29
Q

HCO3- ions are transported [out/into] the RBC at respiring tissues

A

out

30
Q

HCO3- ions are transported out of RBC by… (process)

A

facilitated diffusion

31
Q

___ is taken in when HCO3- exits RBC

A

Cl-

32
Q

a [incr/decr] in pH causes haemoglobin to release O2

A

decr

33
Q

what is another function of haemoglobin other than transporting O2?

A
  • it functions as a pH buffer protein by absorbing H+
  • this prevents a drop in pH
34
Q

H+ in plasma comes from the ________ of carbonic acid

A

H+

35
Q

what does carbonic acid dissociate to form?

A

HCO3- and H+

36
Q

why must the pH of blood be regulated?

A

for optimal enzymatic activity!

37
Q

____________ detect changes in blood pH

A

chemoreceptors

38
Q

what is the function of chemoreceptors?

A

they detect changes in blood pH

39
Q

chemoreceptors send _____________ to the ________

A

nerve impulses, medulla oblongata

40
Q

which part of the brain controls ventilation?

A

the respiratory control centre in the medulla oblongata

41
Q

where are chemoreceptors found?

A
  • in the medulla oblongata
  • in the aorta and carotid arteries
42
Q

how is CO2 released from blood into the lungs for exhalation? (3)

A
  • dissolved CO2 in blood plasma directly enters alveoli
  • carbaminohaemoglobin dissociates to release CO2 from haemoglobin
  • HCO3- from plasma is exchanged for Cl- ions in RBC –> forms carbonic acid with H+ in RBC
    • carbonic acid is converted to H2O and CO2 by carbonic anhydrase to be released into plasma
43
Q

carbonic acid catalyses a ________ reaction (think about the rxn it catalyses!)

A

reversible

44
Q

give a possible scenario that would cause pH in blood to drop

A

exercise

45
Q

how can one improve lung vital capacity?

A

regular exercise

46
Q

how does the body react to a drop in blood pH

A
  • ventilation rate incr + heart rate incr
    • for quicker removal of CO2
    • and for increased O2 uptake to support cell resp
47
Q

what muscles are involved in ventilation? (recap of core)

A

intercostal muscles, diaphragm and abdominal muscles

48
Q

to increase ventilation rate, where nerve impulses will be sent to?

A

intercostal muscles, diaphragm and abdominal muscles

49
Q

what is the regulated range of blood pH?

A

pH 7.35-7.45

50
Q

blood pH is regulated by…

A

homeostatic control

51
Q

when blood pH <7.35, __________ occurs

A

acidosis

52
Q

at what pH does alkalosis occur?

A

pH >7.45

53
Q

what components in blood act as pH buffers?

A

plasma proteins and RBC

54
Q

what is the Bohr shift? (defin.)

A

it is when the oxygen dissocation curve shifts right reflecting a decr oxygen affinity as a result of incr acidity

55
Q
A
56
Q

a decr in pH causes oxygen affinity in haemoglobin to [incr/decr]

A

decr

57
Q

what causes the oxygen dissociation curve to shift right?

A
  • when cells actively respire –> release more CO2 into blood
  • CO2 converted into carbonic acid by carbonic anhydrase
  • lowers the pH of blood
  • causes O2 affinity of RBC to decr –> haemoglobin releases O2 at same partial pressures
58
Q

when the oxygen dissociation curve shifts right, haemoglobin releases [more/less] O2 at ________ partial pressures

A

more, the same

59
Q

how do RBCs know when to release more oxygen?

A
  • at O2 deficient regions, CO2 conc is high –> pH decr
  • haemoglobin’s affinity to O2 decr –> releasing O2
60
Q

why is the Bohr shift important?

A

it ensures that respiring tissues get enough oxygen

61
Q

at higher altitudes, there is [more/less] O2 in atmosphere

A

less

62
Q

the partial pressure of O2 in atmosphere in the mountains is ________

A

lower

63
Q

under what conditions is haemoglobin not fully saturated?

A

at high altitudes

64
Q

how does the respiratory system respond in high altitudes?

A
  • incr ventilation rate
  • incr heart rate
65
Q

if you climb a mountain and you haven’t climbed any mountain before what kind of illness will you get

A

mountain sickness

66
Q

what are some symptoms of mountain sickness

A

nausea, dizziness, headache, fatigue

67
Q

how does the body acclimatise to high altitudes? (apply) (5)

A
  • incr production of RBC
  • incr haemoglobin in RBC
  • muscles produce more myoglobin
  • vital capacity of lungs incr
  • incr in capillaries in muscles and lungs

HL Bio (53 decks)

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