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Cardiopulmonary I > Hemoglobin - White > Flashcards

Hemoglobin - White Flashcards

1
Q

Human RBCs carry how many liters of O2 per day?

A

500-1000 depending on level of activity

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2
Q

% of Hb synthesized before extrusion of nucleus

A

65%

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3
Q

What makes the remaining Hb required for RBC?

A

Reticulocyte

35%

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4
Q

95% of all protein synthesis in reticulocytes is?

A

Globin synthesis

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5
Q

Where are RBCs made during development?

A

Yolk sac
Liver (much lesser extent in spleen)
Bone marrow

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6
Q

Normal Hb adult male

A

14-18 g/dl

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7
Q

Normal Hb adult female

A

12-16 g/dl

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8
Q

Normal Hb newborn

A

11-16 g/dl

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9
Q

Normal Hb child

A

12-15 g/dl

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10
Q

During what ages does Hb increase?

A

5 to 17 years

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11
Q

After what age do males have higher Hb?

A

12 years

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12
Q

Hb Structure

A

One heme per subunit

Four protoporphyrin IX rings

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13
Q

4 types of globin chains in the normal adult

A

alpha
beta
delta
gamma

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14
Q

97% of Hb in adult is

A

HbA a2B2

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15
Q

2 alpha like chains

A

zeta

alpha

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16
Q

4 beta like chains

A

epsilon
gamma
delta
beta

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17
Q

Beta globin genes chromosome

A

Chr 11

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18
Q

Alpha globin genes chromosome

A

Chr 16

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19
Q

All normal Hbs have an a-chain

A

Embryonic

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20
Q

Embryonic Hb

A

Expressed in yolk sac, but not after 8 weeks gestation

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21
Q

3 types of embryonic Hb

A

Hb Gower 1 (z2E2)
Hb Gower 2 (a2E2)
Hb Portland (z2y2)

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22
Q

Fetal Hb

A

HbF
Predominantly in liver
90-95% total Hb production until 34-36 wk gestation
(a2y2)

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23
Q

Adult Hb

A

After birth a2B2 production starts
Reaches adult levels by 1 year
HbA (a2B2)
HbA2 (a2d2)

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24
Q

What controls switch from fetal to adult Hb?

A

Time

So premature infants switch later after both than full term babies

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25
Q

Fetal Hb chains

A

HbF (a2y2)

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26
Q

Adult Hb chains

A

HbA (a2B2)

HbA2 (a2d2)

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27
Q

Sickle Cell Anemia

A

HbS

AA position 6 - glutamic acid to valine

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28
Q

Hemolytic anemia

A

Sickle shaped RBCs

Impede circulation

29
Q

Sickle cell anemia treatment

A

Hydroxyurea
-induces HbF and address inflammation
BUT bad SE

30
Q

Globin gene expression

A

Genear are arranged in linear fashion 5’ to 3’

Arranged in same way they are expressed in life

31
Q

What gives blood its color?

A

Heme

32
Q

Where is heme in Hb?

A

Hydrophobic crevice of the protein chain

33
Q

% of globin chain forms a-helix

A

75%

34
Q

Organic component of heme

A

Protoporphyrin

35
Q

Protoporphyrin is made up of

A 
4 methyl groups
4 pyrrole rings
2 vinyl groups
2 propionate side chains
1 iron atom in middle
36
Q

Subunit structure of Hb

A

8 helical segments

Labeled A through H

37
Q

F8 histidine

A

The proximal histidine which is bound to the heme group

38
Q

E7 histidine

A

The distal histidine and O2 binds to the heme and distal histidine

39
Q

Histidines around the heme iron

A

Proximal F8 - Fe2+ - O2 - H bonded to Distal E7

40
Q

Distal histidine

A

Stabilizing bound oxygen

41
Q

Conformational change

A

Oxygen binding changes the position of the iron ion

0.4 A change

42
Q

Oxygen binding changes

A

The Hb conformation

Upon oxygenation, the iron ion moves into the plane of the heme and pulls down the proximal F8 histidine residue of Hb

43
Q

Myoglobin

A

One heme - Fe2+ - can carry and hold onto 1 O2

Storage protein

44
Q

Myoglobin oxygen dissociation curve

A

To the left and higher

45
Q

P50 of Hb

A

Oxygen partial pressure at which molecule is 1/2 saturated with O2
26

46
Q

Torr to get myoglobin to release 50% of O2 (P50)

A

2.8

47
Q

Oxygen dissociation curve when exercising

A

Drop from 40 torr to 20 torr

Very effective in providing oxygen to exercising tissues

48
Q

Positive cooperativity

A

Hb bind O2 in a cooperative fashion

Conformational change induces change in next

49
Q

Reversibility

A

As Hb loses O2 in tissue, the loss of an oxygen molecule by a globin subunit makes it more likely the next subunit will lose its next molecule

50
Q

Modulators of Fb function

A

2,3-BPG

-an intermediate by product of glycolysis

51
Q

2,3-BPG

A

Signal to Hb to let go of O2

Present in RBCs at approx the same conc as Hb

52
Q

Without 2,3-BPG

A

Hb would be an extremely inefficient oxygen transporter

53
Q

What does 2,3-BPG do to the ODC

A

Shifts it to right

54
Q

No 2,3-BPG

A

Lungs

High affinity for O2

55
Q

High 2,3-BPG

A

Tissues

Low affinity for O2

56
Q

The Bohr Effect

A

pH of actively respiring tissues is lower

Drops from 7.4 to 7.2

57
Q

What happens to pH when exercising

A

Decreases from 7.4 to 7.2

More O2 is released

58
Q

HbF

A

Higher affinity for O2

Does not bind well to 2,3-BPG so has higher affinity for O2

59
Q

T form of Hb

A

Tense/tight form
Low affinity for O2
In non-oxygenated Hb, beta chains are farther apart

60
Q

R form of Hb

A

Relaxed form
High affinity for O2
In oxygenated Hb, beta chains are closer together

61
Q

High 2,3-BPG associated with which form of Hb

A

T form

Low affinity

62
Q

What form of Hb is HbF?

A

R form
Does not bind 2,3-BPG effectively
High affinity

63
Q

2,3-BPG in smokers

A

Higher

Why they get winded going up stairs

64
Q

Smokers form of Hb

A

T state

O2 carrying capacity reduced

65
Q

Sequential model of cooperativity

A

As each oxygen is loaded, causes adjacent globin chain to change from the T to R state

66
Q

Concerted model of cooperativity

A

All Hb tetramers exist in either T or R state
No oxygen bound - T state
Fully loaded - R state

67
Q

Carboxyhemoglobin

A

Occurs when heme is combined with carbon monoxide
210x stronger bond
Impairs transport of O2 to tissue

68
Q

HbA1c

A 
Post translational modification of glucose with the N-terminus of the B-globin chain
Irreversible
3% is normal
Increased in 2-3x in diabetics 
Glucose control for 120 days

Cardiopulmonary I (34 decks)

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