Hemoglobin Flashcards
1
Q
It is a globular protein known consisting of two different pairs of polypeptide chains and four heme groups
A
Hemoglobin
2
Q
Hemoglobin concentration
A
34 g/dL
3
Q
Hemoglobin molecular weight
A
64,000 daltons
4
Q
First and most studied proteins in the body that is easily isolated from red cells
A
Hemoglobin
5
Q
Heme
A
Protoporphyrin
6
Q
Globin
A
4 globin chains
7
Q
Measurement unit for Hgb
A
g/dL
8
Q
Normal value of hemoglobin
A
34 g/dL
9
Q
Real name/complete name of heme
A
Ferroprotoporphyrin IX
10
Q
Where is hemoglobin production takes place
A
Inside the cell (mitochondria)
11
Q
How many enzymes are involved?
A
7
12
Q
Each hemoglobin must contain __ heme molecules
A
4
13
Q
Disorder about individual’s heme production specifically in the production of protoporphyrin IX
A
Porphyria
14
Q
Lacks porphobilinogen deaminase
A
Acute intermittent porphyria
15
Q
Also known as the Ferroprotoporphyrin IX
A
Heme molecule
16
Q
Composition of Heme molecules
A
Protoporphyrin IX and Iron (Fe+)
17
Q
Central atom contains ferrous iron
A
Protoporphyrin IX
18
Q
Ring or carbon, hydrogen, and nitrogen atoms forms the
A
Pyrrole Ring structure
19
Q
Serves as the catch basin for Iron
A
Pyrrole Ring
20
Q
Reversible combines with one O2 molecule
A
Iron (Fe+)
21
Q
Reduced, functional form of hemoglobin
A
Ferrous iron (Fe2+)
22
Q
Oxidized, non-functional form of hemoglobin
A
Ferric iron (Fe3+)
23
Q
Occurs in the mitochondria and cytoplasm of PRONORMOBLAST until RETICULOCYTE SERIES
A
Biosynthesis
24
Q
2 steps under biosynthesis
A
- heme production
- addition of iron
25
Begins with glycine and succinyl A then goes several enzymatic reactions forming protoporphyrin IX that will joined by iron
Heme production
26
Whose responsible for the delivery of Fe3+ iron to pronormoblast
Transferrin
27
a sorting organelle
endosome
28
occurs at the endosome separating ferric iron from transferrin
Acidification
29
making heme
Fe3+ iron is transported to mitochondria to become Fe2+ iron to be reunited with protoporphyrin IX
30
making the hemoglobin molecule
heme leaves mitochondria and joins the globin chain in the cytoplasm
31
Designated by ____ letters and identifiable amino acid chain base pair number
Greek
32
Variations of amino acid sequence give rise to different types of ____
polypeptide chain
33
Chromosome 16
can produce alpha and zeta globin chains
34
Chromosome 11
beta, delta, gamma, epsilon globin chains
35
Coded in the short arm of chromosome
Chromosome 11 and 16
36
Production of globin chain takes place in the ___
nucleus and ribosomes of erythroid cells
37
gene to mRNA occurs in the nucleus
Transcription
38
mRNA to globin occurs in the ribosome
Translation
39
_____ 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
transcription; translation
40
After translation, globin chains formed will be released from ____
ribosomes
41
It is the one that adjusting in order to balance with beta
alpha
42
Alpha
141 amino acids
43
Beta
146 amino acids
44
Gamma A
146 (position 136: alanine)
45
Gamma G
146 (position 136: glycine)
46
Delta
146
47
Epsilon
146
48
Zeta
141
49
Theta
Unknown
50
Genetic abnormalities in the hemoglobin molecule
Hemoglobin variants
51
are used for presumptive tests of any type of hemoglobin
Hemoglobin electrophoresis and HPLC
52
Normal reference values for Men
13.5 to 18.0 g/dL
53
Normal reference values for Women
12.0 to 15.0 g/dL
54
Normal reference values for Newborn
16.5 to 21.5 g/dL
55
Important demographic
age and gender
56
Portland
2 zetas; 2 gammas
embryonic phase
0%
0%
57
Gower I
2 zetas; 2 epsilon
embryonic phase
0%
0%
58
Gower II
2 alphas; 2 epsilon
embryonic phase
0%
0%
59
Fetal
2 alphas; 2 gammas
newborn and adult
60-90%
1-2%
60
Hemoglobin A1
2 alpha; 2 betas
newborn and adult
10-40%
>95%
61
Hemoglobin A2
2 alphas; 2 deltas
newborn and adult
< 0.05%
3.5%
62
Hemoglobin A1c is also known as ____ and ____ accounts for ____ population of Hgb A
glycosylated
glycated hemoglobin
4-6%
63
correlations of diabetes
glycosylated
glycated hemoglobin
64
functional hemoglobin readily binds to ____
O2 molecule
65
how many ml of O2 is bound for every gram of hemoglobin with a ___ mg of Iron
1.34 ml of O2
3.47 mg of Iron
66
The affinity of hemoglobin O2 relates to the _____ defined as the amount of O2 needed to saturate 50% of hemoglobin.
partial pressure
67
Normal O2 affinity
27 mmHg
68
shift to the left
<27 mmHg (increase O2 affinity)
69
shift to the right
> 27 mmHg (decrease O2 affinity)
70
shows the P50 value in sigmoidal curve
dissociation curve
71
shift to the left: ____ O2 affinity to hemoglobin, O2 is ____
increased
NOT released
72
shift to the right: ___ O2 affinity to hemoglobin, O2 is ____
decreased
released
73
factors affecting the dissociation curve
1. oxyhemoglobin
2. deoxyhemoglobin
74
O2 is not released to the tissues
Oxygenated or relaxed state
75
O2 is released to the tissues
Deoxygenated or tense state
76
There's a destruction of salt bridges
Oxyhemoglobin
77
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 ____
alpha-1 and beta-2
disruption of the salt bridges
2,3-BPG
77
___ binds in the beta globin chains forming salt bridges to stabilize the tetramer that decreases the _____
2,3-BPG
affinity of oxygen to hemoglobin
78
Haldane effect
ability of deoxygenated hemoglobin to carry more CO2 than in O2 state
79
Bohr effect
describes hemoglobin lower affinity to oxygen secondary to increase in partial pressure of CO2
80
Acidic in nature
carbon dioxide
81
Blood pH
SL: Increased (Alkali)
SR: Decreased
82
Oxygen affinity
SL: Increased
SR: Decreased
83
Carbon dioxide
SL: Decreased
SR: Increased
84
Temperature
SL: Decreased
SR: Increased
85
2,3-BPG/DPG
SL: Decreased
SR: Increased
86
Shift to the Left associated conditions:
Alkalosis
low body temperature
blood transfusion
increased carboxyhemoglobin
methemoglobinemia
87
Shift to the right associated conditions:
acidosis
high body temperature
hypoxic conditions
88
affinity of oxygen in presence of pressure
partial oxygen
89
unable to transport oxygen
Dysfunctional hemoglobin
90
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
dysfunctional hemoglobin
91
types of dyshemoglobin
1. methemoglobin
2. sulfhemoglobin
3. carboxyhemoglobin
92
formed by reversible oxidation of ferrous iron to become ferric iron
methemoglobin
93
color of blood for methemoglobin
chocolate brown
94
toxic levels of methemoglobin
<25% may be asymptomatic
>30% cyanosis and hypoxic states
>50% comatose or death
95
Methemoglobin is assayed by spectral absorption analysis through absorption at ___ nm
630
96
Clinical condition indicating an increased in methemoglobin
Methemoglobinemia
97
Known as toxic methemoglobinemia; occurs in normal individual after exposure to an oxidant such as ____
Acquired methemoglobinemia
nitrites, primaquine, dapsone
98
treatment for acquired methemoglobin
removal of oxidant
99
due to mutation in CYB5R3 or deficiency in Cytochrome b5 reductase 3
hereditary methemoglobin
100
hemoglobin M that occupies ___ of total hemoglobin population
30-50%
101
produces irreversible change in the polypeptide chains of oxidized hemoglobin
sulfhemoglobin
102
combines with carbon monoxide to form carboxysulfhemoglobin
sulfhemoglobin
103
sulfhemoglobin color of blood
mauve lavender (green)
104
sulfhemoglobin assayed by spectral absorption analysis through absorption at ___ nm
630
105
sulfhemoglobin causes:
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
carbon monoxide combines with heme that has 210-240x more affinity to hemoglobin compared with oxygen
carboxyhemoglobin
107
known as silent killer
carbon monoxide
108
odorless and colorless gas and causes hypoxic states
carbon monoxide
109
shifts the dissociation curve to the left further increasing its affinity and severely impairing release of oxygen to the tissue
carboxyhemoglobin
110
carboxyhemoglobin color of blood
cherry red
111
often have carboxyhemoglobin
smokers
112
carboxyhemoglobin assayed by spectral absorption analysis through absorption at __nm
540
