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HEMATOLOGY 1 > Hemoglobin > Flashcards

Hemoglobin Flashcards

1
Q

Hemoglobin reference range for children (8 to 13 y.o.) in conventional units,

A

12 to 15 g/dL

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2
Q

Hemoglobin reference range for children (8 to 13 y.o.) in S.I. units,

A

120 to 150 g/L

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3
Q

Hemoglobin reference range for adult males in conventional units,

A

14 to 18 g/dL

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4
Q

Hemoglobin reference range for adult males in S.I. units,

A

140 to 180 g/L

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5
Q

Hemoglobin reference range for adult females in conventional units,

A

12 to 15 g/dL

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6
Q

Hemoglobin reference range for adult females in S.I. units,

A

120 to 150 g/L

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7
Q

Main component of red blood cells, comprising 95% of cytoplasmic content,

A

Hemoglobin

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8
Q

Another name for hemoglobin,

A

Respiratory pigment

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9
Q

Concentration of hemoglobin within RBCs,

A

Approximately 34 g/dL

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10
Q

Molecular weight of hemoglobin,

A

Approximately 64,000 Daltons

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11
Q

Scientist who identified hemoglobin as a respiratory protein,

A

Felix Seyler (1862)

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12
Q

Percentage of hemoglobin produced before the RBC nucleus is extruded,

A

0.65

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13
Q

Percentage of hemoglobin synthesized in early reticulocytes,

A

0.35

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14
Q

Most common complex organic molecule in vertebrates,

A

Hemoglobin

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15
Q

Volume of O₂ carried by 1 gram of hemoglobin,

A

1.34 mL

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16
Q

Amount of iron carried by 1 gram of hemoglobin,

A

3.47 mg

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17
Q

Components of a complete adult hemoglobin molecule,

A

1) Globin (protein component) 2) Four protoporphyrin IX molecules 3) Four iron atoms in the ferrous form (Fe+2) 4) One 2,3-BPG molecule

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18
Q

Number of amino acids in alpha globin chain,

A

141

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19
Q

Number of amino acids in beta globin chain,

A

146

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20
Q

Number of amino acids in delta globin chain,

A

146

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21
Q

Number of amino acids in gamma A globin chain,

A

146 (position 136: alanine)

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22
Q

Number of amino acids in gamma G globin chain,

A

146 (position 136: glycine)

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23
Q

Number of amino acids in epsilon globin chain,

A

146

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24
Q

Number of amino acids in zeta globin chain,

A

141

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25
Q

Function of 2,3-BPG in hemoglobin,

A

Delivery of oxygen to tissues

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26
Q

Function of hemoglobin in relation to CO2,

A

Carries waste product CO2 away from the lungs

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27
Q

Function of hemoglobin in relation to nitric oxide (NO),

A

Binding, inactivation, and transport of NO

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28
Q

Amino acid sequence of the polypeptide chains structure,

A

Primary structure of hemoglobin

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29
Q

Chain arrangements in helices and non-helices,

A

Secondary structure of hemoglobin

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30
Q

Arrangement of the helices into a pretzel-like configuration or formation,

A

Tertiary structure of hemoglobin

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31
Q

Complete hemoglobin molecule: spherical, four heme groups attached to four polypeptide chains, carrying up to four molecules of oxygen,

A

Quaternary (tetramer) structure of hemoglobin

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32
Q

Reference method for hemoglobin determination,

A

Cyanmethemoglobin (HiCN) Method

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33
Q

Key reagents in Drabkin’s reagent,

A

Potassium ferricyanide (K3Fe(CN)6), Potassium cyanide (KCN)

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34
Q

Measurement wavelength for HiCN,

A

540 nm (spectrophotometer)

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35
Q

Time for full conversion of hemoglobin to cyanmethemoglobin,

A

10 minutes at room temperature

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36
Q

Types of hemoglobin measured by HiCN method,

A

All types of Hb except sulfhemoglobin

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37
Q

Reaction in the cyanmethemoglobin method,

A

Hemoglobin (Fe2+) + K3Fe(CN)6 → methemoglobin (Fe3+) + KCN → cyanmethemoglobin

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38
Q

Correction for high WBC count (> 20 x 10^9),

A

Centrifuge reagent-sample solution, then measure the supernatant

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39
Q

Correction for high platelet count (> 700 x 10^9),

A

Use lipemic plasma solution

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40
Q

Correction for lipemia,

A

Add 0.01 mL of patient’s plasma to 5 mL of cyanmethemoglobin reagent and use this as the reagent blank

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41
Q

Correction for Hb S and Hb C cells,

A

Dilute 1:2 with distilled water and multiply the results by 2

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42
Q

Correction for abnormal globulins (e.g., plasma cell myeloma, Waldenstrom macroglobulinemia),

A

Add 0.1 gram of potassium carbonate to cyanmethemoglobin reagent

43
Q

Modification to cyanmethemoglobin reagent to prevent abnormal globulin precipitation,

A

Commercially available cyanmethemoglobin reagent contains KH2PO4 salt, preventing this issue

44
Q

Cyanmethemoglobin reagent storage sensitive to light,

A

Store in a brown bottle or dark place

45
Q

Alternative technique for hemoglobin measurement in automated instruments without producing toxic wastes,

A

Uses sodium lauryl sulfate (SLS) to transform hemoglobin to SLS-methemoglobin

46
Q

Example of handheld system for hemoglobin measurement,

47
Q

HemoCue hemoglobin measurement method,

A

Converts hemoglobin to azidemethemoglobin and reads photometrically at two wavelengths (570 nm and 880 nm)

48
Q

Electrophoresis definition,

A

Movement of charged particles in an electric field

49
Q

Primary screening procedure to detect variant hemoglobins,

A

Cellulose Acetate (pH 8.4-8.6)

50
Q

Charge of hemoglobin in alkaline buffer (pH 8.4-8.6),

A

Negatively charged

51
Q

Direction of hemoglobin migration in electrophoresis,

A

Toward the anode (+)

52
Q

Fastest hemoglobin in cellulose acetate electrophoresis,

53
Q

Fast hemoglobins (abnormal/rarely found),

A

Bart Hb, HbH, HbI

54
Q

Slowest hemoglobins in cellulose acetate electrophoresis,

A

Hgb C, A2, E, C (harlem), Hb O (arab)

55
Q

Migration pattern of Hb S, Hb D, and Hb G in cellulose acetate electrophoresis,

56
Q

Point of application in electrophoresis,

57
Q

Purpose of Citrate Agar (pH 6.0 to 6.2) electrophoresis,

A

Confirm variant hemoglobins and differentiate Hb S from D and G, and Hb C from E, OArab, CHarlem

58
Q

Complementary procedure to cellulose acetate Hb electrophoresis,

A

Citrate Agar

59
Q

Hemoglobin synthesis: Heme synthesis,

A

Occurs in mitochondria of metabolically active cells

60
Q

Heme composition,

A

Ferroprotoporphyrin IX, a porphyrin pigment

61
Q

Site of heme synthesis,

A

Mitochondrion

62
Q

Heme biosynthesis location,

A

Prominent in bone marrow and liver

63
Q

Major heme-forming tissue,

A

Erythroid marrow (85% of daily heme requirement)

64
Q

Key enzyme in heme synthesis,

A

Ferrochelatase (Heme synthetase)

65
Q

Function of Ferrochelatase,

A

Inserts Fe 2+ into the protoporphyrin IX ring

66
Q

First step in heme biosynthesis,

A

condensation of succinyl-CoA and glycine by ALAS to generate ALA

67
Q

Globin synthesis site

A

Ribosomes in the normoblast cytoplasm

68
Q

Chromosome for Alpha and Zeta globins

A

Chromosome 16

69
Q

Chromosome for Beta, Delta, Gamma, and Epsilon globins

A

Chromosome 11

70
Q

Embryonic hemoglobins

A

Portland, Gower I, Gower II

71
Q

Embryonic hemoglobin (Portland) Molecular structure:

A

2 zeta, 2 gamma

72
Q

Embryonic hemoglobin (Gower I) Molecular structure:

A

2 zeta, 2 epsilon

73
Q

Embryonic hemoglobin (Gower II) Molecular structure:

A

2 alpha, 2 epsilon

74
Q

Predominant in fetus and newborns

75
Q

Hgb F Proportion in newborns

76
Q

Hgb A1 Proportion in newborns

77
Q

Hgb A2 Proportion in newborns

78
Q

Hgb F Proportion in adults

79
Q

Hgb A1 Proportion in adults

80
Q

Hgb A2 Proportion in adults

81
Q

Hgb F Structure

A

2 alpha, 2 gamma

82
Q

Hgb A1 Structure

A

2 alpha, 2 beta

83
Q

Hgb A2 Structure

A

2 alpha, 2 delta

84
Q

Oxyhemoglobin

A

Hb with Fe2+ and oxygen, found in arterial blood, bright red color

85
Q

Oxyhemoglobin function

A

Transports oxygen from lungs to tissues

86
Q

Oxyhemoglobin conformation

A

R state (relaxed) when oxygenated

87
Q

Deoxygenated hemoglobin

A

Hb with Fe2+, not bound to oxygen, found in venous blood, dark red color

88
Q

Deoxygenated hemoglobin function

A

Transports carbon dioxide from tissues to lungs

89
Q

Deoxygenated hemoglobin conformation

A

T state (tense) when deoxygenated

90
Q

Carboxyhemoglobin

A

Hb with Fe2+ bound to carbon monoxide (CO)

91
Q

Carboxyhemoglobin affinity

A

CO has 240x greater affinity for Hb than oxygen

92
Q

Carboxyhemoglobin gas properties

A

Colorless, odorless, tasteless gas

93
Q

Carboxyhemoglobin poisoning symptoms

A

Cherry red color in blood and skin

94
Q

Main cause of carbon monoxide poisoning

A

Automobile exhaust is the #1 cause of CO exposure

95
Q

Methemoglobin (Hi)

A

Hb with Fe3+, not bound to oxygen

96
Q

Methemoglobin blood color

A

Chocolate brown color in blood

97
Q

Methemoglobin formation

A

Occurs due to oxidation of Fe2+ to Fe3+

98
Q

Methemoglobin health impact

A

Prevents oxygen binding, leading to hypoxia

99
Q

Sulfhemoglobin (SHb)

A

Mixture of oxidized and partially denatured Hb forms

100
Q

Sulfhemoglobin causes

A

Prolonged constipation, enterogenous cyanosis, bacteremia, caused by C. perfringens

101
Q

Sulfhemoglobin color

A

Mauve lavender color

102
Q

Sulfhemoglobin in vitro formation

A

Forms when hydrogen sulfide is added to Hb

103
Q

Sulfhemoglobin in vivo formation

A

Forms due to oxidation by certain drugs and chemicals

104
Q

Sulfhemoglobin risks

A

Can lead to decreased oxygen delivery due to irreversible nature

HEMATOLOGY 1 (29 decks)

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