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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
Q

Diamox

A 
Acetazolamide
inhibits carbonic anhydrase-causes buildup of carbonic acid
decreases pH
His and Lys closer
Gives O2 more readily
26
Q

NO binding

A

binds to Fe and Cys 93

Release at deoxygenation- Hb allowed to bind to endothelium-vasodilation and increased blood flow

27
Q

BPG

A 
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
Q

BPG in Hbf and why

A

no bind
histidine 143 to serine
can’t stabilize T
keep oxygen

29
Q

allosteric binders for T and R

A

T=low pH, BPG, CO2

R=high pH, O2

30
Q

HbA, HbF, HbA2, HbA1c

A

a2b2, a2g2, a2d2, a2b2glucose

31
Q

Smoking and Hb

A

CO2 binds to Hb so baby can’t get it

32
Q

CO poisoning

A

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
Q

CO trx

A

A lot of O2, oversaturate

34
Q

glycation to make HbA1c

A

interacts with bpg-lessens affinity
lock out bpg
Good way of testing for diabetes

35
Q

Cytob5

A

Makes methemoglobin (+3) to +2 and can be useful again

36
Q

cyanide poisoning

A

treat with methemblobin(bonds much easier to that than Hb)

37
Q

Malaria

A

Sickleing triggers WBC to kill malaria plasmodium

38
Q

Thalassemias

A

B-alpha aggregate into heinz bodies

A-HbH tetramers form with reduced solubility and lacks allosteric regulation in HbA

39
Q

heme binding AA

A

His

40
Q

CO binding AA

A

His

41
Q

Bohr effect AA

A

His and Asp

42
Q

NO binding AA

A

Cys

43
Q

sickle cell AA

A

Val

44
Q

Co2 binding AA

A

Arg and val

45
Q

BPG bding AA

A

Val, his, his, Lys

46
Q

quaternary structure

A

Arg, lys asp

47
Q

Hba gly

A

Val

48
Q

HbF vs HbA affinity for BPG

A

his

49
Q

Ferrous or ferric

A

ferrous is the one that binds

50
Q

p50 term

A

used to describe oxygen pressure at which Hb or Mb is 50% saturated

51
Q

Greater p50 in regards to O2 affinity

A

lower

52
Q

BPG and OxyHb

A

does not bind

no positive site

53
Q

HPFH

A

Herditary persistence of fetal hemoglobin

BMS I (30 decks)

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