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Hematology > Unit 5 - Hemoglobin Diseases > Flashcards

Unit 5 - Hemoglobin Diseases Flashcards

1
Q

Oxyhemoglobin

A

LOADS oxygen in lungs

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2
Q

What is the affinity for oxygen of oxyhemoglobin

A

High

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3
Q

What form is oxyhemoglobin in?

A

R or Relaxed form

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4
Q

Deoxyhemoglobin

A

UNLOADS oxygen in the tissues

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5
Q

Affinity for oxygen of deoxyhemoglobin

A

Low

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6
Q

What form is deoxyhemoglobin in?

A

T or tense form

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7
Q

What does 2,3 DPG do?

A

Changes oxyhemoglobin into deoxyhemoglobin

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8
Q

Where does 2,3DPG insert itself?

A

Between beta chains of molecule to make deoxyhemoglobin

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9
Q

What does 2,3DPG do to return hemoglobin into oxyhemoglobin?

A

Exits space between beta chains of molecule to make oxyhemoglobin

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10
Q

When 2,3DPG moves out of deoxyhemoglobin, what is this called?

A

Respiratory movement that makes hemoglobin act as diaphragm for oxygen

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11
Q

What does a shift to the right mean?

A

Right = Low Affinity, Release of oxygen

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12
Q

2,3DPG levels in a shift to the right

A

Increased levels

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13
Q

When does hemoglobin unload more oxygen to tissues?

A

In a shift to the right
At same given tissue partial pressure of oxygen

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14
Q

Conditions causing a shift to the right

A

Inc metabolism
Inc temperature
Dec pH
Tissue hypoxia
Inc carbon dioxide

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15
Q

What is a shift to the left?

A

Giving up less oxygen to the tissues
Won’t let go

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16
Q

If the body is under more restful conditions, what way will the curve shift?

A

To the left

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17
Q

When does hemoglobin unload LESS oxygen to the tissues?

A

In a shift to the left
At same given tissue partial pressure of oxygen

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18
Q

Conditions causing shift to the left

A

Dec metabolism
Inc pH
Inc abnormal hgb
Dec carbon dioxide

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19
Q

Bohr effect

A

Effect of pH on hgb-O2 affinity

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20
Q

More acidic = x affinity for oxygen

A

Less

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21
Q

More acidic = x shift of oxygen

A

Right

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22
Q

Acidic situations = x CO2

A

Increased

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23
Q

As hemoglobin unloads oxygen, what can it accept as a blood buffer?

A

Hydrogen ion

24
Q

Chemical variant of hemoglobin definition

A

Hemoglobins with reduced or absent gaseous exchange capacity

25
Q

Examples of chemical variants of hemoglobin

A

Carboxyhemoglobin
Methemoglobin
Sulfhemoglobin

26
Q

Carboxyhemoglobin

A

Carbon monoxide replaces oxygen
Less binding sites for oxygen

27
Q

How does CO bond to hgb compare to O2?

A

CO has a 200x tighter bond than oxygen

28
Q

What color does carboxyhemoglobin produce to the RBC?

A

Cherry red color

29
Q

What causes carboxyhemoglobin?

A

Smoking
Exhaust fumes from fuel bunring

30
Q

Treatment for carboxyhemoglobin

A

Treatment with oxygen

31
Q

What happens if carboxyhemoglobin is not treated?

A

Prolonged anoxia
Can be fatal or cause permanent damage

32
Q

Methemoglobin

A

Chemically oxidized hgb from ferrous to ferric

33
Q

Normally, what percentage of our hemoglobin is methemoglobin?

A

1%

34
Q

What keeps our percentage of methemoglobin in check?

A

Methemoglobin reductase

35
Q

What happens if methemoglobin becomes pathologic?

A

Cyanosis observed

36
Q

What causes methemoglobin

A

Inherited enzyme deficiency
Hemoglobin M
Drugs or dyes

37
Q

What does hemoglobin M do?

A

Mutation that stabilizes Fe+++ state

38
Q

What drugs or dyes cause methemoglobin

A

Aniline dyes (ink, crayons)
Sulfonamides
Nitrates
Lidocaine

39
Q

Treatment of methemoglobin

A

Methylene blue or ascorbic acid

40
Q

Sulfhemoglobin

A

Permanent replacement of oxygen by sulfur

41
Q

Causes of sulfhemoglobin

A

Sulfur containing cathartics
High levels of sulfonamide antibiotics

42
Q

Can routine hemoglobin analysis measure sulfhemoglobin?

A

NO

43
Q

What is the routine hemoglobin analysis

A

Cyanmethemoglobin

44
Q

What can cyanmethemoglobin method not do?

A

Measure sulfhemoglobin

45
Q

What are genetic varaints of amino acid sequence of globin chains

A

Hemoglobin S
Hemoglobin C

46
Q

What are two ways RBCs are removed from circulation

A

Extravascular destruction
Intravascular destruction

47
Q

Example of extravascular destruction

A

Macrophage removal in the spleen

48
Q

Intravascular destruction example

A

Hemolysis

49
Q

Three chemical components of hemoglobin

A

Heme
Iron
globin

50
Q

When macrophage process RBCs, what components of hemoglobin are conserved?

A

Amino acids from globulins and Fe conserved for synthesis of new molecules

51
Q

When RBCs are processed by macrophages, what happens to the heme?

A

Heme is converted into biliverdin
Biliverdin converted to bilirubin
Bilirubin released to blood for additional processing
Liver excretes bilirubin

52
Q

Macrophage processing is what component of hemolysis?

A

Extravascular

53
Q

Haptoglobin

A

CirculatingProtein in circulation that conserves free hemoglobin

54
Q

What happens without haptoglobin?

A

Hgb can pass through the kidneys into urine

55
Q

What happens to prevent hgb excretion?

A

Hgb-haptoglobin complex forms
Too big to be filtered
Liver cells take it up

56
Q

What does the liver cells to to hemoglobin?

A

Processes hemoglobin similar to macrophages

57
Q

What is a marker for IV hemolysis?

A

Decreased haptoglobin

Hematology (12 decks)

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