Oxygen Carriers Flashcards

(152 cards)

1
Q

Assertion

A

Reason

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2
Q

Free haem in solution binds CO with extremely high affinity.

A

The linear Fe–C–O bond geometry is favored in free haem.

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3
Q

The side chains of glutamate and aspartate participate in the Bohr effect.

A

Their pKs lie between 7 and 8.

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4
Q

Histidine residues contribute to buffering capacity in haemoglobin.

A

Histidine has a pK around 6.5 and can bind/release H+.

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5
Q

Foetal haemoglobin binds 2,3-BPG tightly.

A

H143β is replaced with serine in foetal Hb, which repels BPG.

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6
Q

In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.

A

2,3-BPG lowers oxygen affinity of haemoglobin.

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7
Q

Free haem in solution binds CO with extremely high affinity.

A

The linear Fe–C–O bond geometry is favored in free haem.

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8
Q

The side chains of glutamate and aspartate participate in the Bohr effect.

A

Their pKs lie between 7 and 8.

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9
Q

Histidine residues contribute to buffering capacity in haemoglobin.

A

Histidine has a pK around 6.5 and can bind/release H+.

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10
Q

Foetal haemoglobin binds 2,3-BPG tightly.

A

H143β is replaced with serine in foetal Hb, which repels BPG.

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11
Q

In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.

A

2,3-BPG lowers oxygen affinity of haemoglobin.

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12
Q

Free haem in solution binds CO with extremely high affinity.

A

The linear Fe–C–O bond geometry is favored in free haem.

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13
Q

The side chains of glutamate and aspartate participate in the Bohr effect.

A

Their pKs lie between 7 and 8.

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14
Q

Histidine residues contribute to buffering capacity in haemoglobin.

A

Histidine has a pK around 6.5 and can bind/release H+.

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15
Q

Foetal haemoglobin binds 2,3-BPG tightly.

A

H143β is replaced with serine in foetal Hb, which repels BPG.

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16
Q

In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.

A

2,3-BPG lowers oxygen affinity of haemoglobin.

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17
Q

Free haem in solution binds CO with extremely high affinity.

A

The linear Fe–C–O bond geometry is favored in free haem.

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18
Q

The side chains of glutamate and aspartate participate in the Bohr effect.

A

Their pKs lie between 7 and 8.

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19
Q

Histidine residues contribute to buffering capacity in haemoglobin.

A

Histidine has a pK around 6.5 and can bind/release H+.

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20
Q

Foetal haemoglobin binds 2,3-BPG tightly.

A

H143β is replaced with serine in foetal Hb, which repels BPG.

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21
Q

In the absence of 2,3-BPG, haemoglobin’s oxygen affinity is lower.

A

2,3-BPG lowers oxygen affinity of haemoglobin.

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22
Q

Free haem in solution binds CO with extremely high affinity.

A

The linear Fe–C–O bond geometry is favored in free haem.

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23
Q

The side chains of glutamate and aspartate participate in the Bohr effect.

A

Their pKs lie between 7 and 8.

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24
Q

Histidine residues contribute to buffering capacity in haemoglobin.

A

Histidine has a pK around 6.5 and can bind/release H+.

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25
Foetal haemoglobin binds 2,3-BPG tightly.
H143β is replaced with serine in foetal Hb, which repels BPG.
26
In the absence of 2,3-BPG, haemoglobin's oxygen affinity is lower.
2,3-BPG lowers oxygen affinity of haemoglobin.
27
Assertion
Reason
28
Haemoglobin exhibits cooperative oxygen binding.
Subunit interactions allow conformational changes upon oxygen binding.
29
2,3-BPG increases haemoglobin's oxygen affinity.
2,3-BPG binds to deoxyhaemoglobin and stabilizes it.
30
Oxygen binding by myoglobin is affected by pCO2.
Myoglobin is an allosteric protein.
31
Haemoglobin binds CO2 in tissues.
CO2 binds to terminal amino groups forming carbamino compounds.
32
The Bohr effect is observed in myoglobin.
Myoglobin has ionisable side chains sensitive to pH.
33
Haemoglobin exhibits cooperative oxygen binding.
Subunit interactions allow conformational changes upon oxygen binding.
34
2,3-BPG increases haemoglobin's oxygen affinity.
2,3-BPG binds to deoxyhaemoglobin and stabilizes it.
35
Oxygen binding by myoglobin is affected by pCO2.
Myoglobin is an allosteric protein.
36
Haemoglobin binds CO2 in tissues.
CO2 binds to terminal amino groups forming carbamino compounds.
37
The Bohr effect is observed in myoglobin.
Myoglobin has ionisable side chains sensitive to pH.
38
Haemoglobin exhibits cooperative oxygen binding.
Subunit interactions allow conformational changes upon oxygen binding.
39
2,3-BPG increases haemoglobin's oxygen affinity.
2,3-BPG binds to deoxyhaemoglobin and stabilizes it.
40
Oxygen binding by myoglobin is affected by pCO2.
Myoglobin is an allosteric protein.
41
Haemoglobin binds CO2 in tissues.
CO2 binds to terminal amino groups forming carbamino compounds.
42
The Bohr effect is observed in myoglobin.
Myoglobin has ionisable side chains sensitive to pH.
43
Haemoglobin exhibits cooperative oxygen binding.
Subunit interactions allow conformational changes upon oxygen binding.
44
2,3-BPG increases haemoglobin's oxygen affinity.
2,3-BPG binds to deoxyhaemoglobin and stabilizes it.
45
Oxygen binding by myoglobin is affected by pCO2.
Myoglobin is an allosteric protein.
46
Haemoglobin binds CO2 in tissues.
CO2 binds to terminal amino groups forming carbamino compounds.
47
The Bohr effect is observed in myoglobin.
Myoglobin has ionisable side chains sensitive to pH.
48
Haemoglobin exhibits cooperative oxygen binding.
Subunit interactions allow conformational changes upon oxygen binding.
49
2,3-BPG increases haemoglobin's oxygen affinity.
2,3-BPG binds to deoxyhaemoglobin and stabilizes it.
50
Oxygen binding by myoglobin is affected by pCO2.
Myoglobin is an allosteric protein.
51
Haemoglobin binds CO2 in tissues.
CO2 binds to terminal amino groups forming carbamino compounds.
52
The Bohr effect is observed in myoglobin.
Myoglobin has ionisable side chains sensitive to pH.
53
Assertion
Reason
54
Myoglobin binds oxygen.
Myoglobin contains a haem group which allows it to bind oxygen.
55
Haemoglobin has four subunits.
Each haemoglobin molecule is made up of two alpha and two beta chains.
56
Only haemoglobin contains a haem group.
Myoglobin lacks any prosthetic group.
57
Myoglobin is found in red muscles.
It stores and facilitates oxygen transport within muscle cells.
58
Ferrohaemoglobin is unable to bind oxygen.
Ferrohaemoglobin contains iron in the +2 oxidation state.
59
Myoglobin binds oxygen.
Myoglobin contains a haem group which allows it to bind oxygen.
60
Haemoglobin has four subunits.
Each haemoglobin molecule is made up of two alpha and two beta chains.
61
Only haemoglobin contains a haem group.
Myoglobin lacks any prosthetic group.
62
Myoglobin is found in red muscles.
It stores and facilitates oxygen transport within muscle cells.
63
Ferrohaemoglobin is unable to bind oxygen.
Ferrohaemoglobin contains iron in the +2 oxidation state.
64
Myoglobin binds oxygen.
Myoglobin contains a haem group which allows it to bind oxygen.
65
Haemoglobin has four subunits.
Each haemoglobin molecule is made up of two alpha and two beta chains.
66
Only haemoglobin contains a haem group.
Myoglobin lacks any prosthetic group.
67
Myoglobin is found in red muscles.
It stores and facilitates oxygen transport within muscle cells.
68
Ferrohaemoglobin is unable to bind oxygen.
Ferrohaemoglobin contains iron in the +2 oxidation state.
69
Myoglobin binds oxygen.
Myoglobin contains a haem group which allows it to bind oxygen.
70
Haemoglobin has four subunits.
Each haemoglobin molecule is made up of two alpha and two beta chains.
71
Only haemoglobin contains a haem group.
Myoglobin lacks any prosthetic group.
72
Myoglobin is found in red muscles.
It stores and facilitates oxygen transport within muscle cells.
73
Ferrohaemoglobin is unable to bind oxygen.
Ferrohaemoglobin contains iron in the +2 oxidation state.
74
Myoglobin binds oxygen.
Myoglobin contains a haem group which allows it to bind oxygen.
75
Haemoglobin has four subunits.
Each haemoglobin molecule is made up of two alpha and two beta chains.
76
Only haemoglobin contains a haem group.
Myoglobin lacks any prosthetic group.
77
Myoglobin is found in red muscles.
It stores and facilitates oxygen transport within muscle cells.
78
Ferrohaemoglobin is unable to bind oxygen.
Ferrohaemoglobin contains iron in the +2 oxidation state.
79
Which of the following best describes thalassemia? (1)
B
80
In which regions is thalassemia most commonly found? (2)
and Southeast Asia"
81
What does a '-' symbol indicate in alpha thalassemia genetics? (3)
C
82
How many alpha globin genes are there in a normal individual? (4)
C
83
Which of the following is associated with --/-- in alpha thalassemia? (5)
D
84
Which of the following best describes thalassemia? (6)
B
85
Which of the following best describes thalassemia? (7)
B
86
Which of the following best describes thalassemia? (8)
B
87
Which of the following best describes thalassemia? (9)
B
88
Which of the following best describes thalassemia? (10)
B
89
Which of the following best describes thalassemia? (11)
B
90
Which of the following best describes thalassemia? (12)
B
91
Which of the following best describes thalassemia? (13)
B
92
Which of the following best describes thalassemia? (14)
B
93
Which of the following best describes thalassemia? (15)
B
94
Which of the following best describes thalassemia? (16)
B
95
Which of the following best describes thalassemia? (17)
B
96
Which of the following best describes thalassemia? (18)
B
97
Which of the following best describes thalassemia? (19)
B
98
Which of the following best describes thalassemia? (20)
B
99
Which of the following best describes thalassemia? (21)
B
100
Which of the following best describes thalassemia? (22)
B
101
Which of the following best describes thalassemia? (23)
B
102
Which of the following best describes thalassemia? (24)
B
103
Which of the following best describes thalassemia? (25)
B
104
Which laboratory test best distinguishes beta thalassemia trait from iron deficiency anemia?
B
105
In beta thalassemia major, which hemoglobin fraction is markedly increased?
B
106
In beta thalassemia genetics, what do the symbols β+ and β0 indicate respectively?
B
107
In Cooley’s anemia, which laboratory finding is NOT expected?
hypochromic red cells"
108
Deletion of all 4 α genes (genotype --/--) leads to which condition?
D. Hb Barts Hydrops Fetalis syndrome
109
Assertion: Beta thalassemia is most often due to point mutations in the beta globin gene. Reason: The point mutations result in either reduced (β+) or absent (β0) beta chain production.
A
110
What does the '-' symbol denote when describing alpha thalassemia genotypes?
C
111
Which process underlies the pathophysiology of thalassemia?
B
112
In diagnosing beta thalassemia, which investigation most accurately detects abnormal hemoglobin fractions?
A
113
Which clinical feature differentiates beta thalassemia intermedia from the minor form?
B
114
In thalassemia major, which treatment is primarily used to prevent iron overload?
B
115
Assertion: In alpha thalassemia minor, a low mean cell volume (MCV) is typically observed. Reason: The deletion of one or two α genes decreases alpha chain production, resulting in smaller red blood cells.
A
116
Hereditary persistence of fetal hemoglobin (HPFH) is characterized by the continued production of which hemoglobin tetramer?
B
117
What pathological process gives rise to the facial bone deformities seen in thalassemia major?
A
118
Which blood film feature is most typical in Cooley’s anemia?
"Spherocytes"
119
What characteristic laboratory finding is seen in beta thalassemia minor?
B
120
In beta thalassemia, iron overload most critically affects which organ?
B
121
Which treatment offers a potential cure for beta thalassemia major?
D
122
Assertion: Ineffective erythropoiesis in thalassemia results from the precipitation of unmatched globin chains. Reason: This precipitation damages red cell membranes and leads to intramedullary hemolysis.
A
123
Which prenatal diagnostic method is used in thalassemia screening?
B
124
In managing beta thalassemia major, blood transfusions aim to maintain a hemoglobin level above which threshold?
C
125
Which genotype is most likely to manifest as beta thalassemia major?
B
126
Which intervention is indicated for managing hypersplenism in thalassemia patients?
C
127
Assertion: Antenatal diagnosis is critical for thalassemia prevention. Reason: It allows early detection via fetal blood or DNA analysis, informing potential therapeutic abortion decisions.
A
128
In a diagrammatic representation of alpha thalassemia, if the normal genotype is written as 'αα/αα', what is the correct representation for a silent carrier state?
B
129
A genotype depicted as -α/αα in alpha thalassemia is most consistent with which clinical state?
A
130
In beta thalassemia, comparing a β0/β+ genotype with a β0/β0 genotype, what is the expected difference in clinical severity?
A
131
A blood film diagram showing microcytic, hypochromic cells with target cells is most consistent with which diagnosis?
A
132
Which genotype best corresponds to Hb H disease in alpha thalassemia?
C
133
Assertion: Hb Lepore results from a δβ fusion gene. Reason: This fusion leads to an abnormal beta chain production pattern similar to beta thalassemia.
A
134
In alpha thalassemia, a diagram showing a genotype of --/-- corresponds to which hemoglobin variant?
D
135
A diagram depicting bony facial changes (skull bossing) is most indicative of which thalassemia complication?
C
136
In an Hb electrophoresis diagram, which pattern is most typical for beta thalassemia minor?
B
137
In a family pedigree diagram, if both parents are beta thalassemia carriers, which offspring genotype is most often linked to thalassemia major?
B
138
How does ascorbic acid function diagrammatically in the management of thalassemia major?
C
139
Assertion: Splenectomy is sometimes necessary in thalassemia management. Reason: Hypersplenism drives up transfusion requirements by sequestering and destroying red blood cells.
A
140
In diagrams showing gene dosage in alpha thalassemia, deletion of a single α gene typically results in which clinical state?
D
141
Why is Hb Barts (γ4 tetramer) ineffective as an oxygen carrier, as shown in diagrammatic comparisons?
A
142
A timeline diagram of thalassemia major treatment typically shows that after about 10 years of regular transfusions, which complication develops?
B
143
Which endocrine abnormality is most often depicted in diagrams of thalassemia complications?
B
144
According to diagram-based mechanisms, what role does ineffective erythropoiesis play in thalassemia?
A
145
Where does intramedullary hemolysis primarily occur in thalassemia, as depicted in schematic diagrams?
B
146
Assertion: Elevated HbF is a compensatory response in thalassemia major. Reason: Due to deficient beta chain production, the body increases gamma chain production to form HbF.
A
147
In comparing blood films, which diagrammatic features help differentiate thalassemia from iron deficiency anemia?
B
148
In gene notation, what does 'αα/αα' represent in a pedigree chart?
C
149
Which intervention is depicted as reducing tissue iron deposition in thalassemia treatment diagrams?
A
150
Assertion: Genetic counselling is crucial in managing thalassemia. Reason: It aids in risk assessment and informs prenatal diagnosis options for families at risk.
A
151
Which molecular defect distinguishes Hb Constant Spring from other alpha thalassemia variants in diagrammatic representations?
B
152
Which diagram-based indication, following blood transfusion in thalassemia, confirms successful suppression of extramedullary hematopoiesis?
C