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hemoglobin Flashcards

1
Q

hemoglobin (hb) is composed of

A

4 polypeptide subunits
2α and 2β
1 heme in every polypeptide

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2
Q

hemoglobin (hb) is exists in how many and which forms

A

2 forms

T form and R form

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3
Q

hemoglobin (hb) - T form properties

A

Taut form
deoxygenated
low affinity for 02

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4
Q

hemoglobin (hb) - R form properties

A

Relaxed
oxygenated
high affinity for 02 (X300)

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5
Q

hemoglobin (hb) - properties

A
  1. positive cooperativity

2. negative allostery

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6
Q

hemoglobin (hb) - positive cooperativity

A

tetrameric Hb molecule can bind 4 02 molecules and has higher affinity for each subsequent O2 molecule bound

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7
Q

substance that favor taut form over relaxed form (shift curve to right)

A

INCREASED CL-, H+, CO2, 2,3-BPG, TEMPERATURE

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8
Q

fetal hemoglobin subunits

A

2α and 2γ

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9
Q

fetal hemoglobin vs adult (about function)

A

loewer affinity for 2,3-BPG than adult hemoblobin and thus higher affinity for O2

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10
Q

hemoglobin aslo act as

A

a buffer for H+ ions

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11
Q

buffer for H+ ions

A

hemoglobin

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12
Q

hemoglobin modifications - types

A
  1. methemoglobin

2. carboxyhemoglobin

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13
Q

hemoglobin modifications lead to

A

tissue hypoxia from decreased O2 saturation and decreased 02 content

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14
Q

hemoglobin - normal iron status

A

resuced state Fe2+

FERROUS

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15
Q

ferrous hemoglobin

A

Fe2+

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16
Q

ferric hemoglobin

A

Fe3+

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17
Q

methemoglobin

A

oxidized form of Hb (ferric, F3+)

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18
Q

methemoglobin vs normal hemoglobin - iron status

A

normal: resuced state Fe2+ (FERROUS)
methemoglobin: oxidized state Fe3+ (FERRIC)

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19
Q

methemoglobin properties

A
  • it does not bind 02 as readily

- it has increased affinity for cyanide

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20
Q

methoglobinemia may present with

A
  1. cyanosis 2. chocolate-colored blood
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21
Q

methoglobinemia can can be treated with

A
  1. methylene blue

2. vitamin C

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22
Q

how to treat cyanide poisoning (and the mechanism)

A

nitrites followed by thiosulfate

nitrites: hemoglobin –> methoglobin which bind cyanide
thiosulfate: to bind cyanide, forming thiocyanate , which is renally excreted

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23
Q

methoglobinemia may be used

A

to treat cyanide poisoning

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24
Q

substance that cause poisoning by oxidizing F2+ to F3+ (found in)

A
  1. nitrites (from dieaary intake or polluted/high altitude water)
  2. benzocaine
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25
Q

benzocaine poisoning

A

F2+ to F3+

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26
Q

nitrites poisoning

A

F2+ to F3+

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27
Q

methylene blue is used to

A

treat methoglobinemia

28
Q

carboxyhemoglobin

A

form of hemoglobin bound to CO in place of o2

29
Q

CO binds to Hb in the place of …

A

O2

30
Q

carboxyhemoglobin causes

A

decreased oxygen binding capacity with left shift in oxygen hemoglobin dissociation curve

31
Q

carboxyhemoglobin effect on curve

A

left shift in oxygen in oxygen-hemoglobun (and decreased plateau)

32
Q

carboxyhemoglobin causes in tissues

A

decreased O2 unloading in tissues

33
Q

CO vs O2 on Hb

A

CO binds competitively to Hb and with 200X greater affinity than

34
Q

carboxyhemoglobinemia treatment

A

100% 02 and hyperbaric 02

35
Q

how to treat methemoglobinemia

A

methylene blue

36
Q

oxygen-hemoglobin dissociation curve -shape and why

A

sigmoidal shape due to positive cooperativity

37
Q

Myoglobin - structure, properties

A

Myoglobin monomeric and thus does not show positive cooperativity

38
Q

Myoglobin - oxygen-hemoglobin dissociation curve

A

curves lacks sigmoidal appearance

39
Q

right shift of oxygen-hemoglobin dissociation curve causes

A

decreased affinity of Hb for O2

40
Q

right shift oxygen-hemoglobin dissociation curve - purpose

A

facilitates unloading of 02 to tissue

41
Q

oxygen-hemoglobin dissociation curve with fetal hemoglobin and mechanism

A

Fetal Hb has higher affinity for 02 than adult Hb, so its dissociation curve is shifted left

42
Q

oxygen-hemoglobin dissociation curve shift factors

A
  1. H+ 2. CO2 3. Exercise 4. 2,3-BPG
  2. Altitude 6. Temperature
    increased –> right shift
    decreased –> left shift
43
Q

02 content =

equation

A 
O2 content = (O2 binding capacity x saturation) + disolved O2
 = (1.34xHbxSaO2)  +  (0.003xPaO2) 
SaO2=arterial 02 saturation 
PaO2=partial pressure of 02
(0.003xPaO2) = dissolved oxygen 
(1.34xHb) = oxygen binding capacity
44
Q

normally 1 g Hb bind …. 02

A

1.34 ml

45
Q

normal amount of Hb in blood

A

15g/dL

46
Q

cyanosis results when

A

deoxygenated Hb > 5 g/dL

47
Q

02 binding capacity (calculation and result)

A

O2 binging capacity = normal amount of Hb in blood x 1.34 ml = 15g/dL X 1.34ml = 20.1 ml 02/dL

48
Q

02 binding capacity (result) (normally)

A

20.1 ml 02/dL

49
Q

decreased Hd –> O2 content of arterial blood?

A

decreased

50
Q

decreased Hd –> O2 saturation?

A

no change

51
Q

decreased Hd –> arterial PO2?

A

no change

52
Q

02 delivered to tissues (equation)

A

02 delivered to tissues = cardiac output x O2 contain of blood

53
Q

CO poisoning - Hb concentration?

A

normal

54
Q

anemia - Hb concentration?

A

decreased

55
Q

polycythemia - Hb concentration?

A

increased

56
Q

CO poisoning - % saturation of Hd?

A

decreased

57
Q

anemia - % saturation of Hd?

A

normal

58
Q

polycythemia - % saturation of Hd?

A

NORMAL

59
Q

CO poisoning - dissolved O2 (PaO2)?

A

normal

60
Q

anemia - dissolved O2 (PaO2)?

A

normal

61
Q

polycythemia - dissolved O2 (PaO2)?

A

normal

62
Q

CO poisoning - total 02 content?

A

decreased

63
Q

anemia - total 02 content?

A

decreased

64
Q

polycythemia - total 02 content?

A

increased

65
Q

polycythemia - % saturation of Hd?

A

NORMAL

66
Q

CO vs O2 binding on Hb (affinity?)

A

CO has x200 greater affinity

67
Q

Dissolved O2 in blood - equation

A

0.003 x PaO2

respiratory (27 decks)

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