Final: Respiration 4 Flashcards

1
Q

oxygen transport cascade (5)

A
  • ventilation (air)
  • pulmonary diffusion (lungs)
  • circulatory diffusion (blood)
  • muscle diffusion (capillaries)
  • muscle utilization (tissues)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

how does PO2 and PCO2 change from the environment to the tissues (2)

A
  • PO2 decreases from environment to the tissues
  • PCO2 decreases from the tissue to the environment
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

solubility of O2 in aqueous fluids

A
  • low
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

metalloproteins/respiratory pigments

A
  • proteins containing metal ions which reversibly bind to oxygen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

how do respiratory pigments affect oxygen carrying capacity

A
  • increase O2 carrying capacity by 50-fold
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

respiratory pigments: types (3)

A
  • hemocyanins
  • hemerythrins
  • hemoglobins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

respiratory pigments: hemocyanins
- organisms
- metal type
- location
- appearance

A
  • arthropods and molluscs
  • contain copper
  • usually dissolved in hemolymph
  • appears blue when oxygenated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

respiratory pigments: hemerythrins
- organisms
- metal type
- location
- appearance

A
  • worm-like organisms and sea clams
  • contains iron directly bound to protein
  • usually found inside coelomic cells
  • appears violet-pink when oxygenated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

respiratory pigments: hemoglobin
- organisms
- metal type
- location
- appearance

A
  • vertebrates, nematodes, crustaceans, insects
  • globin protein bound to heme molecule containing iron
  • encapsulated in RBCs
  • appears bright red when oxygenated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

hemoglobin structure (2)
- structure (2)
- mutations

A
  • often 2 alpha and 2 beta chains
  • each chain is ~145 amino acids
  • single aa substitutions can have profound effects on function
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

myoglobulin

A
  • type of hemoglobin found in muscles
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what percentage of blood are RBCs

A
  • 30-60% of blood consists of RBCs
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Hb and RBCs

A
  • RBCs encapsulate Hb and transport O2 and CO2
  • allows for fine-tuning of micro-environment around Hb to optimize function
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what is the percentage of physically dissolved O2 and O2 bound to Hb in blood (2)

A
  • 1.5% of O2 is physically dissolved
  • 98.5% of O2 is bound to Hb
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

oxygen equilibrium curve (OEC)

A
  • compares percent saturation of hemoglobin with PO2
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

OEC: shape (2)

A
  • sigmoid shape
  • allows for maximal unloading with a small change in PO2
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

OEC: maximal unloading (2)

A
  • occurs at 50% O2 saturation of Hb (P50)
  • animals alter P50 of hemoglobin to optimize O2 loading and unloading
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

how does the circulatory system respond to O2 stress (exercise, hypoxia, diving) (2)

A
  • RBCs are released from the spleen
  • elevates hematocrit and hemoglobin levels
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

releasing additional RBCs from spleen: advantage (2)

A
  • enhance oxygen uptake and delivery
  • increase O2 carrying capacity in blood
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

releasing additional RBCs from spleed: disadvantage

A
  • viscosity of blood will eventually be too high, decreasing flow of blood
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

hemoglobin molecule stages (3)

A
  • T state
  • R state
  • Hb molecule goes from T state to R state as it is oxygenated
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Hb: T state (2)

A
  • tense state
  • oxygenation of the Hb is difficult
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Hb: R state (2)

A
  • relaxed state
  • O2 can be added to the Hb more easily
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

T –> R state transition (2)

A
  • transition is associated with weakening/breaking of salt bridges within Hb molecule
  • binding of each additional O2 induces a conformational change that relaxes Hb further
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

what are the ideal OEC conditions at the gas exchange surface (2)

A
  • high Hb affinity (low P50) maximizes O2 uptake
  • left-shifted OEC
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

what is the ideal OEC conditions at the tissues (2)

A
  • low affinity Hb (high P50) maximizes tissue O2 delivery
  • right-shifted OEC
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

how does “right shifting” the OEC affect respiration (2)

A
  • P50 is increased
  • facilitates O2 delivery to active tissues producing CO2
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

OEC: pH changes

A
  • decreasing pH reduces O2 affinity by stabilizing the “T state” and right-shifting the OEC
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

what are conditions that affect OEC (5)

A
  • pH
  • PCO2
  • temperature
  • organic phosphates
  • amino acid sequences
30
Q

how does “left shifting” the OEC affect respiration

A
  • P50 is decreased
  • facilitates O2 uptake at the respiratory surface
31
Q

OEC: PCO2 changes

A
  • increased PCO2 reduces oxygen affinity by stabilizing the “T state” and right shifting the OEC
32
Q

OEC: temperature changes

A
  • increase in temperature decreases oxygen affinity by stabilizing “T state” and “right shifting” the OEC
33
Q

what is an advantage of temperature changes in OEC

A
  • promotes oxygen delivery to warm muscles during exercise
34
Q

OEC: organic phosphates (3)

A
  • ATP, GTP, 2,3-DPG
  • increase in [ ] decreases oxygen affinity by stabilizing “T state” and right-shifting the OEC
  • important for fine-tuning blood P50
35
Q

organic phosphate: mammals

A
  • 2,3-DPG
36
Q

organic phosphate: birds

A
  • IP5
37
Q

organic phosphate: reptiles, amphibians, fish

A
  • ATP or GTP
38
Q

when are organic phosphate levels modified (2)

A
  • during exposure to hypoxia
  • during development altering Hb-O2 affinity
39
Q

what therapeutic applications do organic phosphates have (2)

A
  • synthesis makes it difficult to make artificial blood
  • important in extending life of blood and blood banks from days to months
40
Q

OEC: amino acid sequences

A
  • specific amino acid substitutions have large effects on overall blood oxygen affinity
41
Q

fetal Hb (2)

A
  • generally possess blood O2 affinity that is higher than maternal form
  • allows fetus to get O2 from maternal blood
42
Q

what does the amount of O2 stored in the blood depend on (2)

A
  • PO2 of the plasma
  • Hb - oxygen affinity
43
Q

PO2 of the plasma (2)

A
  • amount of “pressure” that oxygen can bring to bear on the system; how much O2 is “trying” to be loaded
  • only dissolved O2 contributes to partial pressure, while bound O2 does not
44
Q

Hb – oxygen affinity

A
  • the affinity of the carrier (Hb) to carry oxygen in any particular set of circumstances
45
Q

what occurs at P50 (2)

A
  • lots of O2 unloading within small change in PO2
  • O2 physically dissolved leaves first, and Hb bound O2 replaces the dissolved O2
46
Q

what occurs to drop P100 to P50

A
  • oxygen “release” during arterial-venous blood transit before entering site of tissues
47
Q

why is so little O2 released before P50

A
  • at 40-100 Torr, Hb has high affinity for O2 and does not “want to” release it
48
Q

Fick equation for O2 delivery

A

MO2 = Q x (CaO2 - CvO2)

49
Q

Fick equation for O2 delivery: Q

A
  • cardiac output
50
Q

Fick equation for O2 delivery: CaO2 - CvO2

A
  • O2 content of arterial and venous blood
51
Q

root effect (3)

A
  • describes how bony fishes (teleosts) exhibit reduction in O2 carrying capacity with increase in CO2 or reduction in pH
  • due to dramatic stabilization of “T state”
  • this acidified blood won’t reach 100 carrying capacity, no matter how high the PO2 is
52
Q

Bohr effect

A
  • Hb oxygen binding affinity is inversely related both to acidity and to the concentration of carbon dioxide
53
Q

swim bladder (4)

A
  • many bony fish have swim bladders that help to maintain neutral buoyancy
  • gas-filled sac
  • increase gas to increase buoyancy and remove gas to decrease buoyancy
  • in most species, the gas used is O2
54
Q

how do fish fill their swim bladder with O2 (2)

A
  • gulp of air
  • O2 excreted from blood
55
Q

depth and pressure in water

A
  • in water, every 10m of depth is an additional 1 atm of pressure
56
Q

swim bladder: gulp of air

A
  • physostomus
57
Q

swim bladder: O2 excreted from the blood (2)

A
  • physoclistus
  • utilize Root effect, gas gland, and countercurrent exchange
58
Q

what is the basic mechanism of O2 addition to the swim bladder (2)

A
  • arterial blood experiences localized acidosis from gas gland production of H+ and CO2
  • “T state” becomes stabilized and drives O2 from Hb, elevating the PO2
  • excess O2 diffuses and inflates the swimbladder lumen
59
Q

how does the rete mirable contribute to swim bladder inflation (2)

A
  • consists of countercurrent arterial and venous capillaries, in close proximity
  • CO2 from venous blood diffuses into arterial blood, contributing to localized acidosis and increase in PO2
60
Q

what is the result of the gas bland and rete mirable on the swim bladder (2)

A
  • PO2 can be up to 30,000 mmHg
  • swim-bladder can inflate with pure O2 at great depths
61
Q

where else can localized acidosis, similar to filling the swim bladder, be found? (2)

A
  • similar structure exists in fish eyes
  • ensures oxygen delivery to this structure to improve ability to see
62
Q

catastrophic decompression (2)

A
  • fish are brought up from great depths to quickly
  • swim bladders rapidly expand due to decrease in pressure
63
Q

how is carbon monoxide (CO) produced

A
  • byproduct of combustion
64
Q

carbon monoxide (CO) and Hb: affinity (2)

A
  • CO binds Hb with affinity 250x higher than O2
  • Hb becomes 100% saturated with CO at PCO = 0.6 mmHg
65
Q

how does CO affect O2 in blood (3)

A
  • CO competes with O2 for binding to Hb
  • decreases effective O2 carrying capacity of blood
  • small [CO] has large effects on the system
66
Q

0-10% CO-Hb symptoms

A
  • no symptoms
67
Q

10-25% CO-Hb symptoms (2)

A
  • headache
  • nausea
68
Q

30-35% CO-Hb symptoms (4)

A
  • drowsiness
  • headache
  • nausea
  • vomiting
69
Q

40% CO-Hb symptoms

A
  • collapse
70
Q

45% CO-Hb symptoms

A
  • brain damage
71
Q

50% CO-Hb symptoms

A
  • death