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Hematology 1 > (P) Week 3: RBC function Part 2 > Flashcards

(P) Week 3: RBC function Part 2 Flashcards

1
Q

What is the main objective of the hexose monophosphate pathway

A

produce reduced glutathione

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2
Q

____________ protects the molecular structure of our hemoglobin by acting against accumulating oxidants and peroxides which destroys cells and deteriorate hemoglobin

A

glutathione

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3
Q

What is the first enzyme involved in the Hexose monophosphate pathway

A

glucose-6-phosphate dehydrogenase

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4
Q

the hemoglobin of individuals with _______________ deficiency is solid, unstable, will crystallize, and precipitate in the cytoplasm of the red cell

A

G6PD deficiency

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5
Q

a large body formation / inclusion seen within rbcs associated with G6PD deficiency

A

Heinz bodies

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6
Q

T or F

Heinz bodies are specific to G6D

A

F (it is also seen in other unstable hgb problems)

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7
Q

2 forms of the hemoglobin

A

T form (Tense)
R form (Relax)

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8
Q

this form of hgb is unoxygenated

A

T form

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9
Q

this form of hgb is oxygenated

A

R form

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10
Q

at what angle does hgb twist at in order to let 2,3-DPG molecule exit, so that oxygen may enter and bind to the heme

A

15 deg

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11
Q

When the oxygen is delivered to the tissues and organ, hgb twists at what angle to squeeze out the remaining oxygen?

A

zero deg

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12
Q

T or F

Hgb F, composed of 2 alpha and 2 beta globin chains may enter to either T or R form

A

F (Hgb A1)

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13
Q

What form of Hgb twists to a zero deg angle

A

T form

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14
Q

what form of Hgb twists to a 15 deg angle?

A

R form

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15
Q

what is the normal blood pH

A

7.35-7.45

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16
Q

during hypoventilation we suffer from _________ (acidosis / alkalosis)

A

acidosis

less breathing = more CO2 on bloodstream

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17
Q

co2 binding with water to create carbonic acid makes the blood (acidic / alkaline)

A

acidic

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18
Q

during hyperventilation we suffer from (acidosis / alkalosis)

A

alkalosis

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19
Q

decreased CO2 in the blood leads to (acidosis / alkalosis)

A

alkalosis

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20
Q

this mechanism of our bodies does it best to compensate and return our blood pH within normal levels (7.35 - 7.45)

A

compensatory mechanism

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21
Q

T or F

Lungs, Kidneys, and RBC itself aid in maintaining blood pH at normal levels

A

T

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22
Q

what is the partial pressure of residual oxygen in the RBC

A

40 mmHg

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23
Q

T or F

even if there’s still residual oxygen in the RBC, they may still be referred to as unoxygenated RBC

A

T

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24
Q

What is the partal pressure of the lugs

A

100-120 mmHg

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25
Q

As you go to a place with a higher altitude, the oxygen pressure in the lungs ___________causing a person to have a difficulty in breathing

A

decreases

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26
Q

oxygen in the lungs is able to enter the RBC via what process?

A

simple diffusion

lungs (high pressure) to RBC (low pressure)

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27
Q

oxygenated RBC’s oxygen pressure is at

A

100 mmHg

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28
Q

What is the oxygen saturation of oxygenated RBCs with 100 mmHg of pressure

A

95-97%

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29
Q

how many atoms of oxygen does an oxygenated Hgb carry?

A

4 atoms

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30
Q

whenever oxygen (____ charged) is given off to the tissue, hemoglobin may now assume a ______ charge

A

positive charge
negative charge

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31
Q

what enzyme aids the binding of CO2 and H2O?

A

carbonic anhydrase

remember: CO2 + H2O = H2CO3 / carbonic acid

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32
Q

what does the hgb’s negative charge attracts from the tissue, causing for its acidity to slightly increase?

A

one hydrogen atom

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33
Q

____________ is formed due to the loss of one hydrogen atom in the carbonic acid

A

bicarbonate (HCO3)

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34
Q

a phenomenon described as the release of oxygen from the Hgb to the tissue, and the binding of the H+ ion

A

Bohr effect

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35
Q

T or F

acidosis = increased bicarbonate

A

f (increased carbon dioxide)

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36
Q

T or F

In cases of alkalosis, the Hgb holds onto the oxygen to prevent the absorption of a H+ molecule, promoting the further production of carbonic acid as it will not be converted to bicarbonate

A

T

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37
Q

term used for when the blood loses its negative charge

A

chloride shifting

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38
Q

T or F

carbon dioxide directly binds to the Hgb

A

f (it shouldn’t directly bind as it will create bubbles in the blood because it’s a gas)

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39
Q

T or F

in the lungs, Hgb is more attracted to CO2

A

F (oxygen)

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40
Q

the break down of carbonic acid into water and Co2, by carbonic anhydrase, is done where?

A

alveoli

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41
Q

what are the stages do CO2 go through in order to be released outside our body

A

bicarbonate -> carbonic acid -> (broken down by carbonic anhydrase) -> carbon dioxide to be released

42
Q

70% of carbon dioxide that is carried in the lungs is in the

A

plasma bicarbonate

43
Q

20% of carbon dioxide that is carried
in the lungs is in the

A

erythrocyte bicarbonate

44
Q

The remaining 10% of carbon dioxide is transported into two other ways.

a. dissolved and binds with the n-terminal to amino acid from ________________
b. The other 5% is transported in other solutions

A

carbaminohemoglobin

45
Q

the phenomenon that prevents CO2 in the lungs to go back to the Hgb

A

Haldane effect

46
Q

T or F

CO2 is more attracted to the hemoglobin if it is unoxygenated

A

T

47
Q

____________ is inserted into your finger to measure oxygen saturation

A

oximeter

48
Q

how is the normal curve of oxygen illustrated as in oxygen dissociation curve?

A

solid line

49
Q

if you’ve reached 50% oxygen saturation, how much pressure is needed to reach normal levels of o2 saturation?

A

26-27 mmHg

50
Q

What is the normal pressure needed to reach 100% o2 saturation?

A

60-80 mmHg of pressure

51
Q

what type of curve is produced in the oxygen dissociation curve when it has reached a plateau?

A

sigmoid curve

52
Q

shifting to which side in the oxygen dissociation curve indicate that your body needs more oxygen?

A

to the right

53
Q

T or F

the oxygen dissociation curve will shift to the left when your body is in acidosis

A

F (right)

54
Q

An increased release of ______ to the tissue causes the oxygen dissociation curve to shift to the right

A

oxygen

55
Q

a/an __________ release of oxygen to the tissue causes the oxygen dissociation curve to shift to the left

A

decreased

56
Q

shift to the left or right?

hyperthyroidism

A

shift to the right

57
Q

shift to the left or right?

hypothyroidism

A

shift to the left

58
Q

shift to the left or right?

hypercapnia

A

shift to the right

59
Q

shift to the left or right?

low blood pH

A

shift to the right

60
Q

shift to the left or right?

hypocapnia

A

shift to the left

61
Q

hyperthermia

A

shift to the right

62
Q

shift to the left or right?

high blood pH

A

shift to the left

63
Q

shift to the left or right?

high 2,3 DPG level

A

shift to the right

64
Q

shift to the left or right?

hypocapnia

A

shift to the left

65
Q

shift to the left or right?

low 2,3 DPG level

A

shift to the left

66
Q

shift to the left or right?

methemoglobin

A

shift to the right

67
Q

shift to the left or right?
Hgb F

A

shift to the left

68
Q

shift to the left or right?

carboxyhemoglobin

A

shift to the left

69
Q

shift to the left or right?

hemoglobin chesapeake

A

shift to the left

70
Q

shift to the left or right?

hemoglobin s

A

shift to the right

71
Q

shift to the left or right?

hemoglobin kansas

A

shift to the right

72
Q

disease associated with the formation of sulfhemoglobin

A

clostridium perfringens infection

73
Q

The counterpart of Hgb kansas

A

hgb chesapeake

74
Q

facilitates the binding of the hgb in the tissue where the pCO2 is high, an the release of carbon dioxide in the lungs when pCO2 is low

A

Haldane effect

75
Q

protein similar to hgb, it has globin chains and heme, and oxygen also binds to it, but it has a different structur

A

myoglobin

76
Q

composed of single chain of 154 amino acids that forms eight alpha helices and one heme or protoporphyrin IX

A

myoglobin

77
Q

myoglobin molecular weight

A

17,000 daltons

78
Q

hgb molecular weight

A

64,000 daltons

79
Q

hemoglobin : sigmoidal
myoglobin : ________________

A

hyperbolic

80
Q

2 forms of myoglobin

A

deoxymyoglobin
oxymyoglobin

81
Q

T or F

Myoglobin immediately releases the oxygen

A

F (does not, in fact, it binds strongly to the oxygen)

82
Q

T or F

myoglobin releases the oxygen ring only if the oxygen tension in the muscle is severely decreased

A

T

83
Q

clinical use of myoglobin

A

identification of rhabdomyolysis

84
Q

other name for rhabdomyolysis

A

crush syndrome

85
Q

________ levels of myoglobin in the blood indicates rhabdomyolysis / crush syndrome

A

increased

86
Q

Parasite that can destroy the muscles, increases myoglobin levels in the blood

A

trichinella spiralis

87
Q

type of hemolysis wherein macrophages kill senile red cells in the spleen

A

extravascular hemolysis

88
Q

type of hemolysis where senile rbcs die in the circulation

A

intravascular hemolysis

89
Q

condition secondary to red cells dying earlier than the expected life span (120 days)

A

hemolytic anemia

90
Q

pls study heme catabolism again

A

kung ayaw mo edi wag *eyeroll

91
Q

what is the product of heme catabolism

A

bilirubin

92
Q

this becomes unconjugated bilirubin in extravascular hemolysis

A

porphyrin

93
Q

what aids unconjugated bilirubin to travel to the liver

A

albumin

94
Q

proteins responsible to carry the hemoglobin for it to be converted to biliverdin nd bilirubin

A

haptoglobulin
hemopexin
metheme

95
Q

bacteria in the large intestine will convert bilirubin to either

A

stercobilin or urobilinogen

96
Q

these parameter(s) increase in cases of hemolytic anemia

A

bilirubin and methemalbumin

97
Q

pathway that anaerobically generates ATP

A

EMP

97
Q

parameter(s) that are decreased in cases of hemolytic anemia

A

haptoglobulin and hemopexin

98
Q

What HMP shunt product detoxify peroxides

A

NADPF and reduced glutathione

99
Q

if you’re a concrete sequential worker

A

give nath a kith

Hematology 1 (28 decks)

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