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Hematology 1 Discussion > CHAPTER 4 > Flashcards

CHAPTER 4 Flashcards

1
Q

HEMOGLOBIN

RBC
vit and minerals

A

35%

65%

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2
Q

Molecular weight:

A

64,000 Daltons

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3
Q

Respiratory pigment: gives the red color to the blood

A

HEMOGLOBIN

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4
Q

 1 gm Hb can carry (?) O2
 1gm Hb can carry (?) Fe

A

1.34 ml

3.47 mg

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5
Q

 Represents (?) of the total body weight

A

> 1%

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6
Q

 It occupies (?) of the red cell mass ([?]O2)

A

28%

72%

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7
Q

HB BIOSYNTHESIS Regulated by

A

oxygen tension in the kidneys
Hormones
Enzymes in the heme synthesis pathway

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8
Q

FUNCTION
 Lungs –
 Tissues –

A

100 mmHg

20 mmHg

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9
Q

– imp for gas exchange

A

Ca and CO2

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10
Q

COMPONENTS

A

Globin chain

Heme group

2, 3 BPG

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11
Q

Globin chains

A

 2 Alpha Chains
 2 Beta Chains

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12
Q

Dimer

A

Globin chain

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13
Q

Determines the type of Hb

A

Globin chain

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14
Q

The difference in the globin chain relates both to the
(?) in the chain.

A

sequence and to the number of amino acids

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15
Q

Heme =

A

Protoporphyrin IX + Fe+2

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16
Q

141

A

A
Z

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17
Q

Unknown

A

E

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18
Q

146

A

B
D
G

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19
Q

Portland

A

ZG

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20
Q

Gower 1

A

ZE

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21
Q

Gower 2

A

AE

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22
Q

HbF

A

AG

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23
Q

HbA1

A

AB

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24
Q

HbA2

A

AD

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25
Q

Occurs in the mitochondria and cytoplasm of bone marrow erythrocyte precursors

A

HEME SYNTHESIS

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26
Q

Organ for removing:

A

spleen + macrophages

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27
Q

STAGES

A
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28
Q

Iron is delivered to reticulocyte by transferrin

A

Iron Delivery and Supply

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29
Q

Inside the mitochondria

A

Synthesis of Protoporphyrins

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30
Q

Mediated by erythropoietin and vit B6

A

Synthesis of Protoporphyrins

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31
Q

Recycling

A

Hb Degradation

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32
Q

Separation of globin (transported) and heme (further processing)

A

Hb Degradation

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33
Q

Cellular respiration; alters O2 carrying capability

A

2, 3 DIPHOSPHOGLYCERATE (DPG)

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34
Q

90% of tot energy needed by rbcs

A

2, 3 DIPHOSPHOGLYCERATE (DPG)

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35
Q

Major pathway

A

2, 3 DIPHOSPHOGLYCERATE (DPG)

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36
Q

2, 3 DIPHOSPHOGLYCERATE (DPG) PATHWAY

A

Rapoport-Luebering Shunt

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37
Q

Regulates Hemoglobin affinity to O2

A

2, 3 DIPHOSPHOGLYCERATE (DPG)

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38
Q

Facilitate the unloading oxygen from Hb in the tissues

A

2, 3 DIPHOSPHOGLYCERATE (DPG)

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39
Q

Breakdown of the RBC (splenic culling, phagocytosis)

A

ERYTHROCYTE DESTRUCTION

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40
Q

Toward the end of 120 day life span of the RBC, it begins to break down.

A

ERYTHROCYTE DESTRUCTION

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41
Q

The membrane becomes

A

less flexible

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42
Q

The concentration of cellular hemoglobin

A

increases

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43
Q

Enzyme activity, especially glycolysis,

A

diminishes

44
Q

Occurs when hb breaks down in the blood and free hb is released into plasma

A

Intravascular Hemolysis (10%)

45
Q

Free hb binds to the haptoglobin, hemopexin and albumin and engulfed by macrophages.

A

Intravascular Hemolysis (10%)

46
Q

Intravascular Hemolysis (10%) Laboratory:

A

o Increased plasma Hb
o Serum Bilirubin
o Serum Lactose
Dehydrogenase
o Decreased serum
haptoglobin

47
Q

amino acids go back to the amino acid pool

A

GLOBIN

48
Q

Fe & Protoporphyrin

A

HEME

49
Q

: split off and removed by its attachment to a B-1- globulin

A

Iron

50
Q

Iron - reused carried by

A

transferrin

51
Q

Iron - stored

A

(ferritin or hemosiderin)

52
Q
  • broken at the alpha methene bridge by heme oxygenase
A

Protoporphyrin ring

53
Q
  • imp in the liver andspleen
A

Protoporphyrin ring

54
Q
  • biliverdin and CO
A

Protoporphyrin ring

55
Q

NORMAL HEMOGLOBINS

A

EH
HbF
HbA1
HbA2

56
Q

first 3 months after conception

A

Embryonic hemoglobins

57
Q

= analogue of alpha chain

A

zeta chain

58
Q

= counterpart of the
gamma, beta and delta chains.

A

epsilon chain

59
Q

Major Hb of the fetus and the newborn infant

A

Hb F

60
Q

Acid and alkali resistant

A

Hb F

61
Q

Measured by

A

Alkali Denaturation & Kleihauer- Betke Acid Elution.

62
Q

HbF %

After birth, smaller amounts of HbF are produced
- 6 months = HbF is less than
- After age 2 years = HbF less than
- Adults = less than

A

8%

2%

1%

63
Q

HbA1 %

A

97%

64
Q

HbA2 %

A

1.5 - 3.5%

65
Q

HbA2

A

B-Thalassemias, hyperthyroidism and in some cases of megaloblastic anemia

66
Q

Formed when the RBCs pass through the alveolar capillaries of the lungs.

A

Oxyhemoglobin (HbO,)

67
Q

The O2 is loosely bound and unstable

A

Oxyhemoglobin (HbO,)

68
Q

Scarlet red or bright red color

A

Oxyhemoglobin (HbO,)

69
Q

Reduced form

A

Deoxyhemoglobin (HbCO2)

70
Q

Dark red color

A

Deoxyhemoglobin (HbCO2)

71
Q

The CO2 binds to the free amino group of the Hb to form
carbaminohemoglobin

A

Deoxyhemoglobin (HbCO2)

72
Q

Cherry red color

A

Carboxyhemoglobin (HbCO)

73
Q

Oxygen molecules bound to heme are replaced by carbon monoxide.

A

Carboxyhemoglobin (HbCO)

74
Q

Chief Sources of CO:

A

automobile exhaust, industrial wastes, tobacco smoking, charcoal burning (10%)

75
Q

CO Endogenous source:

A

< 1%

76
Q

CO Critical Value:

A

5g /100 ml

77
Q

May cause irreversible tissue changes

A
78
Q

= asphyxiation

A

> 50 to 70%

79
Q

(tissues deprived of O2)

A

asphyxiation

80
Q

NaOH test:

A

40% NaOH + EDTA-blood

81
Q

Warm gently

A

NaOH test

82
Q

NaOH test
HbCO
HbCO2

A

Red (+) HbCO
Black-Brown (+)

83
Q

Dilution test:

A

1mlblood+50mlwater

84
Q

Dilution test:

HbCO
HbO2

A

Cherry Red, pink or bluish red
Yellowish red

85
Q

Tannic Acid test:

A

1% Tannic acid

86
Q

Tannic Acid test

HЬСО
HbO2

A

Red precipitate
Black-brown discoloration

87
Q

Reduced iron (oxidized)

A

Methemoglobin/Hemiglobin (Hi)

88
Q

Irreversible

A

Methemoglobin/Hemiglobin (Hi)

89
Q

Iron in the hemoglobin molecule is in the ferric (Fe3) state instead of the ferrous (Fe2) state

A

Methemoglobin/Hemiglobin (Hi)

90
Q

Incapable of combining with oxygen.

A

Methemoglobin/Hemiglobin (Hi)

91
Q

Hi Normal

A

1.5%

92
Q

Hi Daily

A

0.5% - 3%

93
Q
  • Cyanosis
A

1.5 g/dL (10%)

94
Q

chocolate brown color

A

Hi

95
Q

With strong affinity with CN

A

Hi

96
Q

→ HiCN poisoning

A

(CN) + NO2 → Hi + CN

97
Q

Carboxyhemoglobin (HbCO) Treatment:

A

administration of O2 (hyperbaric)

98
Q

Carboxyhemoglobin (HbCO) Absorption wavelenght:

A

576 nm

99
Q

Methemoglobin/Hemiglobin (Hi) Absorption wavelength:

A

630 - 635 nm

100
Q

Most Iron in the body must be in

A

Ferrous state (Fe2+)

101
Q

Binds to oxygen for transport to lungs and body tissues

A

Ferrous

102
Q

is not able to bind hemoglobin but binds to transferrin

A

Ferric iron (Fe3+)

103
Q

measures the amount of Fe3+ bound to Transferrin

A

Serum Iron

104
Q

free iron; indirect

A

Serum Iron

105
Q

total amount of iron that transferrin can bind when fully saturated

A

Total lron binding Capacity (TIBC)

106
Q

Total lron binding Capacity (TIBC) causrd

A

dec iron consumption; improper recycling of Hb

107
Q

indirect measurement of storage iron in tissue and bone marrow

A

Serum Ferritin

Hematology 1 Discussion (11 decks)

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