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Hemoglobin > Hemoglobin > Flashcards

Hemoglobin Flashcards

1
Q

It is a globular protein known consisting of two different pairs of polypeptide chains and four heme groups

A

Hemoglobin

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2
Q

Hemoglobin concentration

A

34 g/dL

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3
Q

Hemoglobin molecular weight

A

64,000 daltons

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4
Q

First and most studied proteins in the body that is easily isolated from red cells

A

Hemoglobin

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5
Q

Heme

A

Protoporphyrin

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6
Q

Globin

A

4 globin chains

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7
Q

Measurement unit for Hgb

A

g/dL

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8
Q

Normal value of hemoglobin

A

34 g/dL

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9
Q

Real name/complete name of heme

A

Ferroprotoporphyrin IX

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10
Q

Where is hemoglobin production takes place

A

Inside the cell (mitochondria)

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11
Q

How many enzymes are involved?

A

7

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12
Q

Each hemoglobin must contain __ heme molecules

A

4

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13
Q

Disorder about individual’s heme production specifically in the production of protoporphyrin IX

A

Porphyria

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14
Q

Lacks porphobilinogen deaminase

A

Acute intermittent porphyria

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15
Q

Also known as the Ferroprotoporphyrin IX

A

Heme molecule

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16
Q

Composition of Heme molecules

A

Protoporphyrin IX and Iron (Fe+)

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17
Q

Central atom contains ferrous iron

A

Protoporphyrin IX

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18
Q

Ring or carbon, hydrogen, and nitrogen atoms forms the

A

Pyrrole Ring structure

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19
Q

Serves as the catch basin for Iron

A

Pyrrole Ring

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20
Q

Reversible combines with one O2 molecule

A

Iron (Fe+)

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21
Q

Reduced, functional form of hemoglobin

A

Ferrous iron (Fe2+)

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22
Q

Oxidized, non-functional form of hemoglobin

A

Ferric iron (Fe3+)

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23
Q

Occurs in the mitochondria and cytoplasm of PRONORMOBLAST until RETICULOCYTE SERIES

A

Biosynthesis

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24
Q

2 steps under biosynthesis

A
  1. heme production
  2. addition of iron
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25
Q

Begins with glycine and succinyl A then goes several enzymatic reactions forming protoporphyrin IX that will joined by iron

A

Heme production

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26
Q

Whose responsible for the delivery of Fe3+ iron to pronormoblast

A

Transferrin

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27
Q

a sorting organelle

A

endosome

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28
Q

occurs at the endosome separating ferric iron from transferrin

A

Acidification

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29
Q

making heme

A

Fe3+ iron is transported to mitochondria to become Fe2+ iron to be reunited with protoporphyrin IX

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30
Q

making the hemoglobin molecule

A

heme leaves mitochondria and joins the globin chain in the cytoplasm

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31
Q

Designated by ____ letters and identifiable amino acid chain base pair number

A

Greek

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32
Q

Variations of amino acid sequence give rise to different types of ____

A

polypeptide chain

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33
Q

Chromosome 16

A

can produce alpha and zeta globin chains

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34
Q

Chromosome 11

A

beta, delta, gamma, epsilon globin chains

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35
Q

Coded in the short arm of chromosome

A

Chromosome 11 and 16

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36
Q

Production of globin chain takes place in the ___

A

nucleus and ribosomes of erythroid cells

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37
Q

gene to mRNA occurs in the nucleus

A

Transcription

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38
Q

mRNA to globin occurs in the ribosome

A

Translation

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39
Q

_____ of alpha globin genes generates more mRNA than beta globin genes resulting to lesser efficiency in the ____ of alpha globin mRNA to balance the amount of alpha and beta globin chains

A

transcription; translation

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40
Q

After translation, globin chains formed will be released from ____

A

ribosomes

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41
Q

It is the one that adjusting in order to balance with beta

A

alpha

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42
Q

Alpha

A

141 amino acids

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43
Q

Beta

A

146 amino acids

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44
Q

Gamma A

A

146 (position 136: alanine)

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45
Q

Gamma G

A

146 (position 136: glycine)

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46
Q

Delta

A

146

47
Q

Epsilon

A

146

48
Q

Zeta

A

141

49
Q

Theta

A

Unknown

50
Q

Genetic abnormalities in the hemoglobin molecule

A

Hemoglobin variants

51
Q

are used for presumptive tests of any type of hemoglobin

A

Hemoglobin electrophoresis and HPLC

52
Q

Normal reference values for Men

A

13.5 to 18.0 g/dL

53
Q

Normal reference values for Women

A

12.0 to 15.0 g/dL

54
Q

Normal reference values for Newborn

A

16.5 to 21.5 g/dL

55
Q

Important demographic

A

age and gender

56
Q

Portland

A

2 zetas; 2 gammas
embryonic phase
0%
0%

57
Q

Gower I

A

2 zetas; 2 epsilon
embryonic phase
0%
0%

58
Q

Gower II

A

2 alphas; 2 epsilon
embryonic phase
0%
0%

59
Q

Fetal

A

2 alphas; 2 gammas
newborn and adult
60-90%
1-2%

60
Q

Hemoglobin A1

A

2 alpha; 2 betas
newborn and adult
10-40%
>95%

61
Q

Hemoglobin A2

A

2 alphas; 2 deltas
newborn and adult
< 0.05%
3.5%

62
Q

Hemoglobin A1c is also known as ____ and ____ accounts for ____ population of Hgb A

A

glycosylated
glycated hemoglobin
4-6%

63
Q

correlations of diabetes

A

glycosylated
glycated hemoglobin

64
Q

functional hemoglobin readily binds to ____

A

O2 molecule

65
Q

how many ml of O2 is bound for every gram of hemoglobin with a ___ mg of Iron

A

1.34 ml of O2
3.47 mg of Iron

66
Q

The affinity of hemoglobin O2 relates to the _____ defined as the amount of O2 needed to saturate 50% of hemoglobin.

A

partial pressure

67
Q

Normal O2 affinity

A

27 mmHg

68
Q

shift to the left

A

<27 mmHg (increase O2 affinity)

69
Q

shift to the right

A

> 27 mmHg (decrease O2 affinity)

70
Q

shows the P50 value in sigmoidal curve

A

dissociation curve

71
Q

shift to the left: ____ O2 affinity to hemoglobin, O2 is ____

A

increased
NOT released

72
Q

shift to the right: ___ O2 affinity to hemoglobin, O2 is ____

A

decreased
released

73
Q

factors affecting the dissociation curve

A
  1. oxyhemoglobin
  2. deoxyhemoglobin
74
Q

O2 is not released to the tissues

A

Oxygenated or relaxed state

75
Q

O2 is released to the tissues

A

Deoxygenated or tense state

76
Q

There’s a destruction of salt bridges

A

Oxyhemoglobin

77
Q

When hemoglobin binds O2, changes in conformation of the hemoglobin tetramer occurs with a change in hydrophobic interactions at the ___ and ___ contact point causing a _____ and release of ____

A

alpha-1 and beta-2
disruption of the salt bridges
2,3-BPG

77
Q

___ binds in the beta globin chains forming salt bridges to stabilize the tetramer that decreases the _____

A

2,3-BPG
affinity of oxygen to hemoglobin

78
Q

Haldane effect

A

ability of deoxygenated hemoglobin to carry more CO2 than in O2 state

79
Q

Bohr effect

A

describes hemoglobin lower affinity to oxygen secondary to increase in partial pressure of CO2

80
Q

Acidic in nature

A

carbon dioxide

81
Q

Blood pH

A

SL: Increased (Alkali)
SR: Decreased

82
Q

Oxygen affinity

A

SL: Increased
SR: Decreased

83
Q

Carbon dioxide

A

SL: Decreased
SR: Increased

84
Q

Temperature

A

SL: Decreased
SR: Increased

85
Q

2,3-BPG/DPG

A

SL: Decreased
SR: Increased

86
Q

Shift to the Left associated conditions:

A

Alkalosis
low body temperature
blood transfusion
increased carboxyhemoglobin
methemoglobinemia

87
Q

Shift to the right associated conditions:

A

acidosis
high body temperature
hypoxic conditions

88
Q

affinity of oxygen in presence of pressure

A

partial oxygen

89
Q

unable to transport oxygen

A

Dysfunctional hemoglobin

90
Q

it may accumulate to toxic levels, after exposure to certain drugs or environmental chemical or gases, offending agent modified the structure of the hemoglobin molecule preventing it from binding oxygen

A

dysfunctional hemoglobin

91
Q

types of dyshemoglobin

A
  1. methemoglobin
  2. sulfhemoglobin
  3. carboxyhemoglobin
92
Q

formed by reversible oxidation of ferrous iron to become ferric iron

A

methemoglobin

93
Q

color of blood for methemoglobin

A

chocolate brown

94
Q

toxic levels of methemoglobin

A

<25% may be asymptomatic
>30% cyanosis and hypoxic states
>50% comatose or death

95
Q

Methemoglobin is assayed by spectral absorption analysis through absorption at ___ nm

A

630

96
Q

Clinical condition indicating an increased in methemoglobin

A

Methemoglobinemia

97
Q

Known as toxic methemoglobinemia; occurs in normal individual after exposure to an oxidant such as ____

A

Acquired methemoglobinemia
nitrites, primaquine, dapsone

98
Q

treatment for acquired methemoglobin

A

removal of oxidant

99
Q

due to mutation in CYB5R3 or deficiency in Cytochrome b5 reductase 3

A

hereditary methemoglobin

100
Q

hemoglobin M that occupies ___ of total hemoglobin population

A

30-50%

101
Q

produces irreversible change in the polypeptide chains of oxidized hemoglobin

A

sulfhemoglobin

102
Q

combines with carbon monoxide to form carboxysulfhemoglobin

A

sulfhemoglobin

103
Q

sulfhemoglobin color of blood

A

mauve lavender (green)

104
Q

sulfhemoglobin assayed by spectral absorption analysis through absorption at ___ nm

A

630

105
Q

sulfhemoglobin causes:

A
  1. exposure to sulfur chemicals in environmental setting
  2. drugs such as sulfanilamide, phenacetin, nitrites, phenylhydrazone
  3. bacterial infection caused by Clostridium perfringens and Clostridium welchii
106
Q

carbon monoxide combines with heme that has 210-240x more affinity to hemoglobin compared with oxygen

A

carboxyhemoglobin

107
Q

known as silent killer

A

carbon monoxide

108
Q

odorless and colorless gas and causes hypoxic states

A

carbon monoxide

109
Q

shifts the dissociation curve to the left further increasing its affinity and severely impairing release of oxygen to the tissue

A

carboxyhemoglobin

110
Q

carboxyhemoglobin color of blood

A

cherry red

111
Q

often have carboxyhemoglobin

A

smokers

112
Q

carboxyhemoglobin assayed by spectral absorption analysis through absorption at __nm

A

540

Hemoglobin (1 decks)

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