Haemoglobin and gas transport Flashcards

1
Q

How much O2 is dissolved in plasma ?

A

3 mL

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2
Q

What is the O2 carrying capacity of blood?

A

200 mL

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3
Q

What is haemoglobin carrying capacity ?

A

197 mL

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4
Q

What determines partial pressure of O2 in plasma?

A

It is determined by O2 solubility in plasma and partial pressure of O2 gas that drives diffusion

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5
Q

What is O2 solubility in plasma?

A

0.03 ml/L/mm Hg

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6
Q

How much plasma do we have per L of blood?

A

3 ml/L

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7
Q

How much blood do we have ?

A

We have from 4.7 to 5L of blood.

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8
Q

What is the O2 demand in tissues?

A

250 ml/min

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9
Q

How much O2 is delivered to tissues per minute?

A

200 x 5 = 1000 ml/min

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10
Q

Describe haemoglobin

A

It consists of 4 polypeptide chains, 2 alpha and 2 beta chains, each has one harm group, so one haemoglobin can carry 4 molecules of O2.

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11
Q

What type of biding is present in haemoglobin with O2?

A

cooperative binding

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12
Q

What is normal haemoglobin O2 saturation?

A

97-98%

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13
Q

What is the major determinant of haemoglobin O2 saturation ?

A

Partial pressure of O2

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14
Q

How long is the contact time and how long is the oxygenation process?

A

contact time is 0.75 s and saturation takes 0.25s

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15
Q

Name all the different types of haemoglobin

A

HbA in RBC, HbA, glycolysated HbA1a, HbA1b, HbA1c, HbA2 variant of HbA, and foetal HbF (still present in adults)

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16
Q

What portion of haemoglobin is HbA?

A

92%

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17
Q

What chains are in HbA?

A

2 alpha and 2 beta

18
Q

What chains are in haemoglobin HbA2?

A

2 alpha and 2 delta

19
Q

What chains are in HbF?

A

2 alpha and 2 gamma

20
Q

At what partial pressure there is big change in O2 saturation ?

A

at 60 mmHg, saturation of 90%

21
Q

What is the O2 saturation at pressure 40 mmHg?

A

The saturation is 75%, it is reserve, can be used when there is high metabolic demand

22
Q

Rank haemoglobin, myoglobin and foetal haemoglobin in terms of affinity for O2

A

myoglobin has the highest affinity, foetal haemoglobin and normal haemoglobin

23
Q

Where is the most of myoglobin present?

A

in oxidative fibres in muscle

24
Q

What partial pressure is called the dead zone and why

A

40 mmHg is dead zone and there is very little gradient for diffusions to tissues

25
What is the effect of anaemia on O2 carrying capacity, saturation and partial pressure of O2?
The total carrying capacity is reduced, but the partial pressure and saturation remains the same
26
What can cause anaemia ?
iron deficiency, B12 deficiency or haemorrhage
27
How can haemoglobin affinity for O2 be reduced( more O2 is given off)?
By low pH, increased PCO2, and increased temperature and added DPG
28
What is DPG?
DPG is diphosphoglycerate, it is produced by RBC as a response to hypoxia. In people living in high altitudes, cardiac and lung problems
29
What is the name of the effect that shift the curve to the right as a response to lower pH etc?
Bohr effect
30
What is the affinity of haemoglobin to CO?
It is 250 x higher than the affinity for O2
31
What is formed when CO binds to haemoglobin ?
carboxyhaemoglobin
32
At what partial pressure carboxyhemoglobin starts to form?
at 0.4 mmHg
33
What are the signs of CO poisoning ?
headache, deep red colour of cheeks, skin and mucous membranes, nausea, confusion, hypoxia
34
Name the 5 types of hypoxia.
Hypoxic hypoxia, anaemic hypoxia, ischaemic, histotoxic and metabolic
35
What causes hypoxic hypoxia ?
Due to reduction in O2 diffusion in lungs either due to low O2 in atmosphere or lung pathology
36
What causes anaemic hypoxia ?
Low level of red blood cells
37
What causes ischaemic hypoxia?
Herat disease and sufficient pumping of blood around the body
38
What causes histotoxic hypoxia?
Poising such as CO
39
What causes metabolic hypoxia?
Increased demand of O2 by tissues which is not met by the supply
40
How is CO2 transported around the body?
Dissolved in plasma 7%, as bicarbonate ion formed in RBC 70%, as carbamino haemoglobin 23%
41
How are bicarbonate ions formed?
CO2 into red blood cells, combine with water forming H2CO3 with the help gof enzyme carbonic anhydrase, dissociate to HCO3- , out to plasma by chloride shift, H+ ions are buffered by deoxyhaemoglobin