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BMS I > hemoglobin +hemoglobinopathies > Flashcards

hemoglobin +hemoglobinopathies Flashcards

1
Q

Hemoglobin Kempsey

A

locks hemoglobin in its high oxygen affinity. Reduces oxygen delivery to tissues. His92Tyr

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2
Q

Sickle Cell Disease

A

Glu6Val. Deoxygenated HBs pol

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3
Q

Heme function

A

Coordinate oxygen increasing solubility

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4
Q

Methemoglobin

A

Oxidized hemoglobin

Treat with CO2

Stopped by histidine E7

Dimerization between two methemoglobins and O

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5
Q

Artificial porfirins

A

Strerically hinder from dimerizing

No antigens

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6
Q

Myoglobin (structure)

A

Catalytic parts (oxygens) of heme on outside, important parts on inside=protects from rusting

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7
Q

p50

A

affinity of molecule for gas

  • increase, forcing gas to interact with molecule
  • pressue where half oxygen molecules bound

Smaller the p50 has higher the affinity

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8
Q

Myoglobin

A

Hyberbolic dissassoctation curve

Kept together by hydrophobic forces

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9
Q

F8 histidine

A

holds heme in place-binds iron in place

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10
Q

iron’s 6 bonds

A

4 to porphyrin rings N’s
1 to oxygen
1 to F8 histidine

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11
Q

E8 histidine

A

Saves us from CO2 poisoning

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12
Q

myoglobin vs hemoglobin p50

A

hyperbolic with lower p50

sigmoidal with higher p50

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13
Q

what holds both alpha chains together

A

Arg 141 with Asp 126 and Lys 127

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14
Q

What causes sinusoidal curve

A

coopertivity

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15
Q

Idealized hemoglobin vs -0 coopertivty

A

all or no coopertivity-looks very sinusoidal

looks like myoglobin

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16
Q

Hill coffecient

A

n=2.8 for hemo
=1 for myo

Coopertivity score

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17
Q

pressure in lungs vs prior

A

100 to 20

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18
Q

T vs R state favor

A

R state favored when 4 O’s
-T state 2 O’s pushes to R state
T state favored when no O’s on
-R state 2 O’s pushes to T state

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19
Q

Allostery direction

A

Inhibition or activation

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20
Q

T vs R state affinintity and why

A

Higher affinity for Oxygen in R

oxygen stabilizes R state

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21
Q

why is T state more stable

A

disulfide bridges-more favorable

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22
Q

increase pH which state is better

A

R state favored, His and Lys move apart due to loss of positive charge on His, can take more oxygen (to stabilize)

23
Q

decrease pH which state better

A

T state favored-gives more O2-His146 and Lys 64 closer

24
Q

Co2 binding

A

Acidifies blood at carbonic acid

Binds to Arg to transport-T state

25
Diamox
``` Acetazolamide inhibits carbonic anhydrase-causes buildup of carbonic acid decreases pH His and Lys closer Gives O2 more readily ```
26
NO binding
binds to Fe and Cys 93 Release at deoxygenation- Hb allowed to bind to endothelium-vasodilation and increased blood flow
27
BPG
``` extremely negative Only binds to T state Helps deliver oxygen Surronded by postive charges Increase at high altitudes Val, his, his, lys More ready to give up o2 ```
28
BPG in Hbf and why
no bind histidine 143 to serine can't stabilize T keep oxygen
29
allosteric binders for T and R
T=low pH, BPG, CO2 R=high pH, O2
30
HbA, HbF, HbA2, HbA1c
a2b2, a2g2, a2d2, a2b2glucose
31
Smoking and Hb
CO2 binds to Hb so baby can't get it
32
CO poisoning
Binds well on heme UNLESS histidine E8 is close to it (bends CO bond) then O2 would much rather bind cuz can make another bond
33
CO trx
A lot of O2, oversaturate
34
glycation to make HbA1c
interacts with bpg-lessens affinity lock out bpg Good way of testing for diabetes
35
Cytob5
Makes methemoglobin (+3) to +2 and can be useful again
36
cyanide poisoning
treat with methemblobin(bonds much easier to that than Hb)
37
Malaria
Sickleing triggers WBC to kill malaria plasmodium
38
Thalassemias
B-alpha aggregate into heinz bodies A-HbH tetramers form with reduced solubility and lacks allosteric regulation in HbA
39
heme binding AA
His
40
CO binding AA
His
41
Bohr effect AA
His and Asp
42
NO binding AA
Cys
43
sickle cell AA
Val
44
Co2 binding AA
Arg and val
45
BPG bding AA
Val, his, his, Lys
46
quaternary structure
Arg, lys asp
47
Hba gly
Val
48
HbF vs HbA affinity for BPG
his
49
Ferrous or ferric
ferrous is the one that binds
50
p50 term
used to describe oxygen pressure at which Hb or Mb is 50% saturated
51
Greater p50 in regards to O2 affinity
lower
52
BPG and OxyHb
does not bind | no positive site
53
HPFH
Herditary persistence of fetal hemoglobin

BMS I (30 decks)

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