NURS 5315 Hematology EXAM
2025/2026 LATEST UPDATE|
COMPREHENSIVE QUESTIONS WITH
100% RATED ANSWERS
1. Which blood component is primarily responsible for oxygen transport?
A) White blood cells
B) Platelets
C) Red blood cells
D) Plasma
Correct ,,,,answer,,,,: C) Red blood cells
Rationale: Red blood cells contain hemoglobin, which binds oxygen and
transports it to body tissues. RBCs are specifically designed for this function with
their biconcave shape and hemoglobin content .
2. What is the main protein in red blood cells that binds oxygen?
A) Albumin
B) Hemoglobin
C) Fibrinogen
D) Myoglobin
,Correct ,,,,answer,,,,: B) Hemoglobin
Rationale: Hemoglobin is the primary oxygen-carrying protein in red blood cells,
essential for oxygen delivery to tissues throughout the body .
3. What structural components make up hemoglobin?
A) One alpha and one beta chain
B) Two alpha and two beta chains
C) Two alpha and two delta chains
D) Three alpha and one beta chain
Correct ,,,,answer,,,,: B) Two alpha and two beta chains
Rationale: Hemoglobin consists of two alpha and two beta globin chains, which
are critical for its function and structural stability. This tetramer structure enables
cooperative oxygen binding .
4. How many oxygen molecules can a single hemoglobin molecule bind?
A) 1
B) 2
C) 3
D) 4
Correct ,,,,answer,,,,: D) 4
,Rationale: Each hemoglobin molecule has four heme groups, and each heme
contains an iron atom that can bind one oxygen molecule, totaling four oxygen
molecules per hemoglobin .
5. What is the significance of the heme group in hemoglobin?
A) Provides structural support
B) Binds carbon dioxide
C) Binds oxygen
D) Activates enzymes
Correct ,,,,answer,,,,: C) Binds oxygen
Rationale: The heme group contains an iron atom that binds oxygen, enabling
hemoglobin to transport oxygen throughout the body .
6. What happens to hemoglobin when oxygen binds to it?
A) It forms methemoglobin
B) It releases iron
C) It undergoes a conformational change
D) It loses its binding affinity
Correct ,,,,answer,,,,: C) It undergoes a conformational change
Rationale: Oxygen binding causes hemoglobin to change shape (conformational
change), increasing its affinity for additional oxygen molecules through
cooperative binding .
, 7. Which effect enhances oxygen unloading from hemoglobin in tissues with
low pH?
A) Haldane effect
B) Bohr effect
C) Krebs effect
D) Hemoglobin effect
Correct ,,,,answer,,,,: B) Bohr effect
Rationale: The Bohr effect describes how acidic conditions (low pH) and high
carbon dioxide levels promote oxygen release from hemoglobin, facilitating
oxygen delivery to metabolically active tissues .
8. What condition is associated with an inability of hemoglobin to bind oxygen
effectively?
A) Deoxyhemoglobin formation
B) Formation of methemoglobin
C) Increased pH levels
D) Elevated heme production
Correct ,,,,answer,,,,: B) Formation of methemoglobin
Rationale: Methemoglobin forms when iron is oxidized to the ferric state (Fe3+),
preventing effective oxygen binding and impairing oxygen delivery to tissues .
2025/2026 LATEST UPDATE|
COMPREHENSIVE QUESTIONS WITH
100% RATED ANSWERS
1. Which blood component is primarily responsible for oxygen transport?
A) White blood cells
B) Platelets
C) Red blood cells
D) Plasma
Correct ,,,,answer,,,,: C) Red blood cells
Rationale: Red blood cells contain hemoglobin, which binds oxygen and
transports it to body tissues. RBCs are specifically designed for this function with
their biconcave shape and hemoglobin content .
2. What is the main protein in red blood cells that binds oxygen?
A) Albumin
B) Hemoglobin
C) Fibrinogen
D) Myoglobin
,Correct ,,,,answer,,,,: B) Hemoglobin
Rationale: Hemoglobin is the primary oxygen-carrying protein in red blood cells,
essential for oxygen delivery to tissues throughout the body .
3. What structural components make up hemoglobin?
A) One alpha and one beta chain
B) Two alpha and two beta chains
C) Two alpha and two delta chains
D) Three alpha and one beta chain
Correct ,,,,answer,,,,: B) Two alpha and two beta chains
Rationale: Hemoglobin consists of two alpha and two beta globin chains, which
are critical for its function and structural stability. This tetramer structure enables
cooperative oxygen binding .
4. How many oxygen molecules can a single hemoglobin molecule bind?
A) 1
B) 2
C) 3
D) 4
Correct ,,,,answer,,,,: D) 4
,Rationale: Each hemoglobin molecule has four heme groups, and each heme
contains an iron atom that can bind one oxygen molecule, totaling four oxygen
molecules per hemoglobin .
5. What is the significance of the heme group in hemoglobin?
A) Provides structural support
B) Binds carbon dioxide
C) Binds oxygen
D) Activates enzymes
Correct ,,,,answer,,,,: C) Binds oxygen
Rationale: The heme group contains an iron atom that binds oxygen, enabling
hemoglobin to transport oxygen throughout the body .
6. What happens to hemoglobin when oxygen binds to it?
A) It forms methemoglobin
B) It releases iron
C) It undergoes a conformational change
D) It loses its binding affinity
Correct ,,,,answer,,,,: C) It undergoes a conformational change
Rationale: Oxygen binding causes hemoglobin to change shape (conformational
change), increasing its affinity for additional oxygen molecules through
cooperative binding .
, 7. Which effect enhances oxygen unloading from hemoglobin in tissues with
low pH?
A) Haldane effect
B) Bohr effect
C) Krebs effect
D) Hemoglobin effect
Correct ,,,,answer,,,,: B) Bohr effect
Rationale: The Bohr effect describes how acidic conditions (low pH) and high
carbon dioxide levels promote oxygen release from hemoglobin, facilitating
oxygen delivery to metabolically active tissues .
8. What condition is associated with an inability of hemoglobin to bind oxygen
effectively?
A) Deoxyhemoglobin formation
B) Formation of methemoglobin
C) Increased pH levels
D) Elevated heme production
Correct ,,,,answer,,,,: B) Formation of methemoglobin
Rationale: Methemoglobin forms when iron is oxidized to the ferric state (Fe3+),
preventing effective oxygen binding and impairing oxygen delivery to tissues .
