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Hematology 1 Discussion > CHAPTER 4 PART 2 > Flashcards

CHAPTER 4 PART 2 Flashcards

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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
After 50 years of age =
slight decrease
26
 (?) in the morning and (¿) in the evening
Higher lower
27
(?) if lying down
Lower
28
 in smokers: high altitude
Increased
29
Determines the proportion of O2, released to the tissues or loaded onto the cell at a given oxygen pressure.
OXYGEN AFFINITY
30
means hemoglobin has an increased affinity for O2, so it binds more and does not want to give it up
Increases in oxygen affinity
31
Decreases in oxygen affinity, cause.
O2 to be released
32
FACTORS AFFECTING HEMOGLOBIN AFFINITY FOR OXYGEN
1. Blood (Body) Temperature 2. Blood pH 3. Level2,3–DPG 4. Carbon Dioxide (Haldane Effect) 5. Fetal Hb 6. Abnormal Hb
33
• Hgb has less attraction or affinity for 02
Right-Shift
34
•Hgb willing to release Oz to totissue. tissue
Right-Shift
35
•Hgb has more attraction for O2
Left shift
36
Hgb less willing to release O2 to tissues
Left shift
37
•Alterations in blood pH, shifts oxygen dissociation curve
Bohr Effect
38
•In acidic pH, the curve shifts to the right
Bohr Effect
39
•Results in an enhanced capacity to release O2 where it is needed
Bohr Effect
40
• Uptake of oxygen will release carbon dioxide
Haldane Effect
41
And losing of oxygen will increase affinity for carbon dioxide
Haldane Effect
42
(quantitative defect)
Thalassemic (quantitative defect) disorders
43
(qualitative defect)
Hemoglobinopathies
44
decreased or non-existent production of one or more globin chain type.
Thalassemic disorders
45
• Alpha • Beta • Alpha and Beta
• Alpha (Asians) • Beta (mediteranean) • Alpha and Beta (African)
46
Result from the alteration of the DNA genetic code for the chains → hemoglobin variants
Hemoglobinopathies
47
– changes 1 or more amino acids in the sequence
1. Substitution
48
– changes in the part of Hb
2. Deletion
49
– joins the DNA sequence
3. Addition/Elongation
50
– joins another amino acid in the sequence
4. Fusion
51
amino acid substitution
Hemoglobin S
52
No HbA is produced
Hemoglobin S
53
Sickling occurs when O2, is reduced at the tissue level.
Hemoglobin S
54
The Hb S molecule polymerizes leading to the formation of (?) which cause the cells to become rigid.
tactoid crystals
55
gene has provided resistance from Plasmodium falciparum
Hemoglobin S
56
Hemoglobin S Polymorphism in Hb genes
(Hb S, Hb E and B- Thalassemia, G- 6PD def.)
57
protects individuals from developing severe falciparum malaria.
Hemoglobin S
58
Hemoglobin S Inheritance:
- Homozygous (SS)- visible - Heterozygous (AS)-not visible
59
o Anemia is usually severe
Sickle Cell Anemia (SS)
60
o increase RDW
Sickle Cell Anemia (SS)
61
Sickle Cell Anemia (SS) o Blood Smear:
Polychromasia, Sickle cells, target cells, ovalocytes, schistocytes; Howell-Jolly & Pappenheimer bodies
62
o Retarded Growth and sexual maturation
Sickle Cell Anemia (SS)
63
Sickle Cell Anemia (SS) o Hbs o HbF o Hb A2, Normal
80-90% 10-20% 1.5-3.5%
64
o Any situation that produces excessive deoxygenation of RBCs
Sickle Cell Crises
65
Sickle Cell Crises o Eg.
Vasoocclusive crises
66
o Hb A compensates for Hb S
Sickle Cell Trait
67
o Patients usually have no symptoms unless in cases of extreme tissue hypoxia
Sickle Cell Trait
68
Sickle Cell Trait o HbS
30-45%
69
Hb s-Thalassemia
 Hb S-a  Hb S-B
70
Other Sickling Hbs same amino acid substitution as HbS with additional unique 6-substitution
Hb C-Harlem; C-Ziguinchor; S-Travis
71
Screening test: sickling hemoglobin
DITHIONITE SOLUBILITY TUBE TEST
72
Red cells are lysed by (?) allowing hb to escape.
saponin
73
binds with oxygen
Sodium dithionite
74
polymerizes and forms a precipitate
Deoxygenated hb S
75
make the solution turbid.
Tactoids
76
Turbidity: against a
newsprint/reader card with thin black lines.
77
Turbidity:
(+) HbS
78
TEST FOR UNSTABLE HbS
1. Isopropanol Pot Test 2. Heat Denaturation/Instability Test (50°C for 3 hrs.) 3. Heinz bodies training (Wright Stain)
79
 N/N anemia with numerous target cells
Hb C Disease (CC)
80
: hexagonal or rod-shaped crystals; blunt ends; rigid cells
 Hb CC crystals
81
RBCs – slightly hypochromic, target cells
HbC Trait (AC)
82
 Milder than Hb SS
Hemoglobin SC disease
83
 "pocketbook" cells
Hemoglobin SC disease
84
: with fingerlike projections.
 Hb SC crystals
85
 Methemoglobin and congenital cyanosis
Hemoglobin M
86
 Amino acid substitution: not protected from oxidation of iron
Hemoglobin M
87
 Cyanosis, Blood: chocolate brown; Heinz bodies
Hemoglobin M

Hematology 1 Discussion (11 decks)

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