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Hematology 1 Discussion > CHAPTER 4 PART 2 > Flashcards

CHAPTER 4 PART 2 Flashcards

1
Q

Production of reduced Diphosphopyridine dinucleotide (DPNH) in the presence of

A

methemoglobin reductase (diaphorase)

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2
Q

Production of reduced Triphosphopyridine nucleotide (TPNH) in the presence of

A

Glucose-6-PO4 dehydrogenase → Reduced Glutathione

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3
Q

o Increase production

A

Inherited Enzyme Deficiency

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4
Q

o NADH-Methemoglobin reductase deficiency or Diaphorase deficiency

A

Inherited Enzyme Deficiency

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5
Q

Results of various amino acid substitutions in the globin chain that directly affect the heme group.

A

Inherited M

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6
Q

Inherited M Acquired: Chemical or therapeutic agents

A

(aniline dyes, NO3, NO2, antimalarial drugs, sulfonamides)

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7
Q

Inherited M Therapy:

A

Ascorbic Acid & Methylthioninium Cl

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8
Q

Org. sulfides + Hb oxidant drugs (phenacetin & acetanilid, sulfonamides)

A

Sulfhemoglobin

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9
Q

Hb oxidant drugs

A

(phenacetin & acetanilid, sulfonamides)

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10
Q

IRREVERSIBLE

A

Sulfhemoglobin

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11
Q

Sulfhemoglobin + CO -

A

Carboxysulfhemoglobin

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12
Q
A

Sulfhemoglobin

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13
Q

Sulfhemoglobin Critical value:

A

0.5 g/100 ml

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14
Q

mauve-lavender (when its stained) Heinz bodies (central stippling)

A

Sulfhemoglobin

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15
Q

Absorption: 600-620 nm

A

Sulfhemoglobin

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16
Q

 ferricyanide + Fe3+ of Hb

A

Cyanmethemoglobin (HCN)

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17
Q

 The most stable among the pigments

A

Cyanmethemoglobin (HCN)

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18
Q

 Absorption wavelength: 540 nm

A

Cyanmethemoglobin (HCN)

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19
Q

“fast hemoglobins”

A

GLYCOSYLATED HEMOGLOBIN

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20
Q

irreversibly glycosylated at 1 or both N-terminal valines (or
lysine) of the B-chains

A

GLYCOSYLATED HEMOGLOBIN

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21
Q

HbA1a, HbA1b, Hb A1c

A

GLYCOSYLATED HEMOGLOBIN

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22
Q

is elevated 2 - 3 fold in patients with diabetes mellitus.

A

Hb A1c

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23
Q

Increased Hb

A

Polycythemia
Dehydration (burns, diarrhea)

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24
Q

Decreased Hb

A

All anemia
Leukemia

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25
Q

After 50 years of age =

A

slight decrease

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26
Q

 (?) in the morning and (¿) in the evening

A

Higher

lower

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27
Q

(?) if lying down

A

Lower

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28
Q

 in smokers: high altitude

A

Increased

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29
Q

Determines the proportion of O2, released to the tissues or loaded onto the cell at a given oxygen pressure.

A

OXYGEN AFFINITY

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30
Q

means hemoglobin has an increased affinity for O2, so it binds more and does not want to give it up

A

Increases in oxygen affinity

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31
Q

Decreases in oxygen affinity, cause.

A

O2 to be released

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32
Q

FACTORS AFFECTING HEMOGLOBIN AFFINITY FOR OXYGEN

A
  1. Blood (Body) Temperature
  2. Blood pH
  3. Level2,3–DPG
  4. Carbon Dioxide (Haldane Effect)
  5. Fetal Hb
  6. Abnormal Hb
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33
Q

• Hgb has less attraction or affinity for 02

A

Right-Shift

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34
Q

•Hgb willing to release Oz to totissue. tissue

A

Right-Shift

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35
Q

•Hgb has more attraction for O2

A

Left shift

36
Q

Hgb less willing to release O2 to tissues

A

Left shift

37
Q

•Alterations in blood pH, shifts oxygen dissociation curve

A

Bohr Effect

38
Q

•In acidic pH, the curve shifts to the right

A

Bohr Effect

39
Q

•Results in an enhanced capacity to release O2 where it is needed

A

Bohr Effect

40
Q

• Uptake of oxygen will release carbon dioxide

A

Haldane Effect

41
Q

And losing of oxygen will increase affinity for carbon dioxide

A

Haldane Effect

42
Q

(quantitative defect)

A

Thalassemic (quantitative defect) disorders

43
Q

(qualitative defect)

A

Hemoglobinopathies

44
Q

decreased or non-existent production of one or more globin chain type.

A

Thalassemic disorders

45
Q

• Alpha
• Beta
• Alpha and Beta

A

• Alpha (Asians)
• Beta (mediteranean)
• Alpha and Beta (African)

46
Q

Result from the alteration of the DNA genetic code for the chains → hemoglobin variants

A

Hemoglobinopathies

47
Q

– changes 1 or more amino acids in the sequence

A
  1. Substitution
48
Q

– changes in the part of Hb

A
  1. Deletion
49
Q

– joins the DNA sequence

A
  1. Addition/Elongation
50
Q

– joins another amino acid in the sequence

A
  1. Fusion
51
Q

amino acid substitution

A

Hemoglobin S

52
Q

No HbA is produced

A

Hemoglobin S

53
Q

Sickling occurs when O2, is reduced at the tissue level.

A

Hemoglobin S

54
Q

The Hb S molecule polymerizes leading to the formation of
(?) which cause the cells to become rigid.

A

tactoid crystals

55
Q

gene has provided resistance from Plasmodium falciparum

A

Hemoglobin S

56
Q

Hemoglobin S

Polymorphism in Hb genes

A

(Hb S, Hb E and B- Thalassemia, G-
6PD def.)

57
Q

protects individuals from developing severe falciparum malaria.

A

Hemoglobin S

58
Q

Hemoglobin S Inheritance:

A
  • Homozygous (SS)- visible
  • Heterozygous (AS)-not visible
59
Q

o Anemia is usually severe

A

Sickle Cell Anemia (SS)

60
Q

o increase RDW

A

Sickle Cell Anemia (SS)

61
Q

Sickle Cell Anemia (SS)

o Blood Smear:

A

Polychromasia, Sickle cells, target cells, ovalocytes, schistocytes; Howell-Jolly & Pappenheimer bodies

62
Q

o Retarded Growth and sexual maturation

A

Sickle Cell Anemia (SS)

63
Q

Sickle Cell Anemia (SS)

o Hbs
o HbF
o Hb A2, Normal

A

80-90%

10-20%

1.5-3.5%

64
Q

o Any situation that produces excessive deoxygenation of RBCs

A

Sickle Cell Crises

65
Q

Sickle Cell Crises o Eg.

A

Vasoocclusive crises

66
Q

o Hb A compensates for Hb S

A

Sickle Cell Trait

67
Q

o Patients usually have no symptoms unless in cases of
extreme tissue hypoxia

A

Sickle Cell Trait

68
Q

Sickle Cell Trait o HbS

A

30-45%

69
Q

Hb s-Thalassemia

A

 Hb S-a
 Hb S-B

70
Q

Other Sickling Hbs same amino acid substitution as HbS with additional unique 6-substitution

A

Hb C-Harlem; C-Ziguinchor; S-Travis

71
Q

Screening test: sickling hemoglobin

A

DITHIONITE SOLUBILITY TUBE TEST

72
Q

Red cells are lysed by (?) allowing hb to escape.

A

saponin

73
Q

binds with oxygen

A

Sodium dithionite

74
Q

polymerizes and forms a precipitate

A

Deoxygenated hb S

75
Q

make the solution turbid.

A

Tactoids

76
Q

Turbidity: against a

A

newsprint/reader card with thin black lines.

77
Q

Turbidity:

A

(+) HbS

78
Q

TEST FOR UNSTABLE HbS

A
  1. Isopropanol Pot Test
  2. Heat Denaturation/Instability Test (50°C for 3 hrs.)
  3. Heinz bodies training (Wright Stain)
79
Q

 N/N anemia with numerous target cells

A

Hb C Disease (CC)

80
Q

: hexagonal or rod-shaped crystals; blunt
ends; rigid cells

A

 Hb CC crystals

81
Q

RBCs – slightly hypochromic, target cells

A

HbC Trait (AC)

82
Q

 Milder than Hb SS

A

Hemoglobin SC disease

83
Q

 “pocketbook” cells

A

Hemoglobin SC disease

84
Q

: with fingerlike projections.

A

 Hb SC crystals

85
Q

 Methemoglobin and congenital cyanosis

A

Hemoglobin M

86
Q

 Amino acid substitution: not protected from oxidation of
iron

A

Hemoglobin M

87
Q

 Cyanosis, Blood: chocolate brown; Heinz bodies

A

Hemoglobin M

Hematology 1 Discussion (11 decks)

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