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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
Fetal Hb chains
HbF (a2y2)
26
Adult Hb chains
HbA (a2B2) | HbA2 (a2d2)
27
Sickle Cell Anemia
HbS | AA position 6 - glutamic acid to valine
28
Hemolytic anemia
Sickle shaped RBCs | Impede circulation
29
Sickle cell anemia treatment
Hydroxyurea -induces HbF and address inflammation BUT bad SE
30
Globin gene expression
Genear are arranged in linear fashion 5' to 3' | Arranged in same way they are expressed in life
31
What gives blood its color?
Heme
32
Where is heme in Hb?
Hydrophobic crevice of the protein chain
33
% of globin chain forms a-helix
75%
34
Organic component of heme
Protoporphyrin
35
Protoporphyrin is made up of
``` 4 methyl groups 4 pyrrole rings 2 vinyl groups 2 propionate side chains 1 iron atom in middle ```
36
Subunit structure of Hb
8 helical segments | Labeled A through H
37
F8 histidine
The proximal histidine which is bound to the heme group
38
E7 histidine
The distal histidine and O2 binds to the heme and distal histidine
39
Histidines around the heme iron
Proximal F8 - Fe2+ - O2 - H bonded to Distal E7
40
Distal histidine
Stabilizing bound oxygen
41
Conformational change
Oxygen binding changes the position of the iron ion | 0.4 A change
42
Oxygen binding changes
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
Myoglobin
One heme - Fe2+ - can carry and hold onto 1 O2 | Storage protein
44
Myoglobin oxygen dissociation curve
To the left and higher
45
P50 of Hb
Oxygen partial pressure at which molecule is 1/2 saturated with O2 26
46
Torr to get myoglobin to release 50% of O2 (P50)
2.8
47
Oxygen dissociation curve when exercising
Drop from 40 torr to 20 torr | Very effective in providing oxygen to exercising tissues
48
Positive cooperativity
Hb bind O2 in a cooperative fashion | Conformational change induces change in next
49
Reversibility
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
Modulators of Fb function
2,3-BPG | -an intermediate by product of glycolysis
51
2,3-BPG
Signal to Hb to let go of O2 | Present in RBCs at approx the same conc as Hb
52
Without 2,3-BPG
Hb would be an extremely inefficient oxygen transporter
53
What does 2,3-BPG do to the ODC
Shifts it to right
54
No 2,3-BPG
Lungs | High affinity for O2
55
High 2,3-BPG
Tissues | Low affinity for O2
56
The Bohr Effect
pH of actively respiring tissues is lower | Drops from 7.4 to 7.2
57
What happens to pH when exercising
Decreases from 7.4 to 7.2 | More O2 is released
58
HbF
Higher affinity for O2 | Does not bind well to 2,3-BPG so has higher affinity for O2
59
T form of Hb
Tense/tight form Low affinity for O2 In non-oxygenated Hb, beta chains are farther apart
60
R form of Hb
Relaxed form High affinity for O2 In oxygenated Hb, beta chains are closer together
61
High 2,3-BPG associated with which form of Hb
T form | Low affinity
62
What form of Hb is HbF?
R form Does not bind 2,3-BPG effectively High affinity
63
2,3-BPG in smokers
Higher | Why they get winded going up stairs
64
Smokers form of Hb
T state | O2 carrying capacity reduced
65
Sequential model of cooperativity
As each oxygen is loaded, causes adjacent globin chain to change from the T to R state
66
Concerted model of cooperativity
All Hb tetramers exist in either T or R state No oxygen bound - T state Fully loaded - R state
67
Carboxyhemoglobin
Occurs when heme is combined with carbon monoxide 210x stronger bond Impairs transport of O2 to tissue
68
HbA1c
``` 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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