Quiz 5 Flashcards

1
Q

What is the process of moving O2 and CO2 in and out of body tissues?

A

Diffusion.

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2
Q

What are the four types of Hypoxia?

A
  1. Hypoxic hypoxia.
  2. Stagnant (ischemic) hypoxia.
  3. Anemic hypoxia.
  4. Histotoxic hypoxia.
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3
Q

Describe and give examples of Hypoxic hypoxia

A

Inadequate O2 uptake into blood in lungs.
Chronic obstructive pulmonary disease.
ex. COPD, O2 supple malfunction.

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4
Q

Describe and give examples of Stagnant (ischemic) hypoxia

A

Inadequate blood flow to an organ.
Arteriosclerosis PVD.
Ex. MI, Embolism

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5
Q

Describe and give examples of Anemic hypoxia

A

Inadequate blood oxygen carrying capacity.
Inactivated hemoglobin.
ex. Low Hct

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6
Q

Describe and give examples of Histotoxic hypoxia

A

Interference with mitochondrial respiration.

ex. cyanide poisoning

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7
Q

How much oxygen do hemoglobin carry compare to plasma?

A

Hgb carries 65 times more O2 than plasma

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8
Q

Describe the Structure of a hemoglobin

A

Oxygen carrier protein with 4 subunits= 2 alpha + 2 beta.

Normal adult Hgb is a2b2.

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9
Q

Each gm of Hb can carry up to how much O2?

A

1gm Hgb can carry 1.31ml of O2

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10
Q

What is the name of hemoglobin once O2 is combined?

A

Oxyhemoglobin

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11
Q

What is dissociation between Hb and O2

A

Critically fast reaction important for O2 exchange.

Very loose coordination bonds between Fe2 and O2

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12
Q

Oxygen saturation definition

A

Ratio of oxygen bound to Hb compared to total amount that can be bound

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13
Q

Oxygen capacity definition

A

Maximal amount of O2 bound to Hb

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14
Q

How many O2 molecules can be bound to one Hgb

A

Four

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15
Q

Rough rule of SpO2 and PO2

A

PO2 40,50,60=SpO2 70,80,90

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16
Q

Pathological Ligands of Hemoglobin

A

Ligands form covalent bonds to the ferrous iron in Hb.

Ex CO 250 times the affinity of O2.
NO 200,000 times the affinity of O2

17
Q

Explain what P50 is

A

The PO2 when hemoglobin is 50% saturated (SpO2=50%)

18
Q

Describe what a Left Shift is and what could cause it

A

More affinity.

Decreased PCO2, Increased pH, Decrease temp,

19
Q

Describe what a Right Shift is and what could cause it

A

Less affinity.
Increase PCO2, Decreased pH, Increase Temp
(all things you will see with active muscles/metabolism.

20
Q

What is the Bohr Effect?

A

An increase in H+ (lower pH) decreases Hb’s affinity for O2.

21
Q

What does stored blood transfusion do to the Hb-O2 dissassociation curve?

A

They are typically stored cold and significantly dimished levels of 2,3 DPG.

This would produce a leftward shift.

22
Q

What is Myoglobin

A

Single chained heme pigment found in skeletal muscle.

Mb stores O2 temporarily in muscle. Has increased affinity for O2.

23
Q

What is CaO2?

A

O2 Content in the blood

24
Q

What is the formula for CaO2

A

CaO2=(SO2 x Hb x 1.31) + (PO2 x 0.003)

25
What is DO2?
DO2=oxygen delivery. | CaO2 x CO
26
What is Carbon dioxide?
Volatile waste product of cellular metabolism
27
Normal CO2 production in resting adult?
200ml/min
28
Carbon dioxide is transported by blood in three forms:
1. Dissolved directly in blood. 2. Bicarbonate ion (HCO3) and Carbonic Acid (H2CO3) *main way. 3. Bound to Hgb and plasma proteins
29
Are CO2 levels effected by V/Q mismatch?
No; Diffusing capacity 20x greater with CO2 than with O2. | Reason why even one lung ventilation is adequate for CO2 removal.
30
Ability of CO2 to bind with Hgb increased or decreased with deoxygenated Hgb? Oxygenated Hgb?
Increased. Decreased.
31
What is the Haldane effect?
Upon binding O2HB releases CO2 and H+ which in turn is converted to CO2.
32
What is the PO2 when the SpO2 is 50%
27