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1. Which RBC membrane protein gives the RBC a negative charge?
A. Spectrin B. Glycophorin C. Ferritin D. Transferrin
B. Glycophorin.
Glycophorin is an integral membrane protein that gives the RBC a negative charge, helping RBCs repel each other instead of sticking together.
2. Glycophorin is what type of membrane protein?
A. Peripheral B. Nuclear C. Integral D. Cytoplasmic
C. integral
Glycophorin is an integral protein, meaning it is embedded in the RBC membrane
Approximately what percentage of total RBC membrane protein is glycophorin?
A. 5% B. 10% C. 20% D. 50%
c. 20%
4. What is the primary function of spectrin?
A. Carries oxygen
B. Stores iron
C. Helps maintain RBC shape and deformability
D. Produces bilirubin
c. helps maintain RBC shape and deformability.
Spectrin is part of the RBC's internal support system. It helps maintain the biconcave shape and allows the RBC to bend and squeeze through tiny vessels
Spectrin is classified as a:
A. Peripheral protein
B. Integral protein
C. Heme protein
D. Plasma protein
A. peripheral protein.
Spectrin is a peripheral membrane protein, meaning it is associated with the inside surface of the RBC membrane.
What does deformability mean?
A. RBCs can divide
B. RBCs can change shape and squeeze through small blood vessels
C. RBCs can make DNA D. RBCs can produce antibodies
B. RBCs can change shape and squeeze through small blood vessels
Which organ removes most old, damaged, and deformed RBCs?
A. Liver B. Kidney C. Spleen D. Lung
C. spleen.
The spleen is especially good at detecting and removing old, damaged, or abnormal RBCs.
An RBC that has lost membrane and becomes round is called a:
A. Target cell
B. Spherocyte
C. Acanthocyte
D. Reticulocyte
B. spherocyte
A spherocyte is an RBC that has lost some of its membrane and becomes more round/spherical instead of biconcave.
Which RBC has irregular, spiny projections called spicules?
A. Spherocyte
B. Target cell
C. Acanthocyte D. Schistocyte
c. Acanthocyte
Acanthocytes have increased membrane:
A. Flexibility
B. Rigidity
C. Permeability to oxygen
D. ATP production
B. Rigidity.
Acanthocytes have a more rigid/stiff membrane, making them less flexible.
12. Which condition is associated with acanthocytes?
A. Abetalipoproteinemia
B. Iron deficiency only
C. Dehydration only
D. Leukemia
A. Abetalipoproteinemia.
Acanthocytes are classically associated with abetalipoproteinemia and can also occur with liver disease
13. A target cell can be associated with an increase in:
A. Cholesterol
B. ATP
C. Hemoglobin
D. Calcium only
A. cholesterol.
Increased cholesterol in the RBC membrane can alter its shape and contribute to target cells.
14. Increased cholesterol can make the RBC membrane more:
A. Flexible
B. Viscous/sticky
C. Porous
D. Thin
B. Viscous/sticky.
Too much cholesterol can make the RBC membrane more viscous, affecting its normal shape.
Target cells can be seen with cholesterol accumulation associated with:
A. Liver disease
B. Kidney stones
C. Asthma
D. Diabetes only
A. liver disease.
Cholesterol accumulation and target cells can be associated with liver disease
Hemoglobin consists of globin and:
A. 1 heme group
B. 2 heme groups
C. 3 heme groups
D. 4 heme groups
D. 4 heme groups.
One hemoglobin molecule has 4 globin chains and 4 heme groups
. Normal adult hemoglobin contains how many globin chains?
A. 2 B. 3 C. 4 D. 6
c. 4 globin chain
. A heme group contains:
A. Globin and calcium
B. Protoporphyrin and Fe²⁺
C. Cholesterol and sodium
D. Albumin and iron
B. protoporphyrin and Fe2+
Which form of iron is found in normal functional heme?
A. Fe⁺ B. Fe²⁺ C. Fe³⁺ D. Fe⁴⁺
B. Fe2+
Normal functional hemoglobin uses Fe²⁺ (ferrous iron) to bind oxygen.
Each globin chain is associated with how many heme groups?
A. 0 B. 1 C. 2 D. 4
B. 1
One hemoglobin molecule can carry how many oxygen molecules?
A. 1 B. 2 C. 3 D. 4
D. 4
There are four heme groups, and each can bind one oxygen molecule. Therefore, one hemoglobin molecule can carry 4 O₂ molecules.
Which three things are needed for normal hemoglobin synthesis?
A. Iron, protoporphyrin, and globin
B. Calcium, cholesterol, and ATP
C. Sodium, potassium, and calcium
D. Albumin, bile, and bilirubin
A. Iron, protoporphyrin, and globin.
All three are needed to make normal hemoglobin.
Globin chains are synthesized on:
A. Mitochondria B. Cytoplasmic ribosomes C. Nucleus only D. Lysosomes
B. Cytoplasmic ribosomes
. What provides the instructions for globin chain production?
A. Genes B. ATP C. Cholesterol D. Bilirubin
A. genes.
Genes provide the instructions for making the different globin chains
Which of the following is NOT a globin chain?
A. Alpha B. Beta C. Gamma D. Ferritin
D. ferritin
Ferritin is an iron-storage protein, not a globin chain
28. During embryonic development, globin production switches from:
A. Alpha → Zeta
B. Zeta → Alpha
C. Beta → Epsilon
D. Gamma → Epsilon
B. Zeta-> Alpha.
During development, globin production switches from the early zeta chain to alpha
29. During development, epsilon globin is replaced by:
A. Gamma, delta, and beta
B. Alpha only
C. Zeta only
D. Ferritin
A. Gamma, delta, and beta
The embryonic epsilon chain is replaced as development progresses by gamma, delta, and beta globin production
30. Normal adult HbA makes up approximately:
A. 1-2%
B. 2-3%
C. 50-60%
D. 95-97%
D. 95-97%
31. HbA is composed of:
A. α₂β₂
B. α₂δ₂
C. α₂γ₂
D. β₂γ₂
A. α₂β₂
HbA contains 2 alpha + 2 beta chains
HbA₂ normally makes up approximately:
A. 1-2%
B. 2-3%
C. 20-30%
D. 95-97%
B. 2-3%
HbA₂ is composed of:
A. α₂β₂
B. α₂δ₂
C. α₂γ₂
D. β₂δ₂
B. α₂δ₂
HbA₂ contains 2 alpha + 2 delta chains
35. HbF normally makes up approximately what percentage of adult hemoglobin according to your notes?
A. 1-2%
B. 2-3%
C. 20-30%
D. 95-97%
A. 1-2%
34. HbF is fetal hemoglobin. It is composed of:
A. α₂β₂
B. α₂δ₂
C. α₂γ₂
D. β₂γ₂
C. α₂γ₂.
HbF contains 2 alpha + 2 gamma chains.
36. The main function of hemoglobin is to:
A. Destroy RBCs
B. Carry and deliver oxygen
C. Make antibodies
D. Store cholesterol
B. carry and deliver oxygen
Hemoglobin's major job is to pick up oxygen in the lungs and deliver it to tissues.
37. Hemoglobin combined with oxygen is called:
A. Methemoglobin
B. Carboxyhemoglobin
C. Oxyhemoglobin
D. Sulfhemoglobin
C. oxyhemoglobin
When hemoglobin is carrying oxygen, it is called oxyhemoglobin
38. Hemoglobin also helps transport CO₂ to the:
A. Spleen B. Bone marrow C. Liver D. Lungs
D. lungs
Hemoglobin helps transport CO₂ back toward the lungs, where it can be exhaled.
39. What controls hemoglobin's affinity for oxygen?
A. 2,3-DPG B. Ferritin C. Albumin D. Bilirubin
A. 2,3-DPG.
2,3-DPG helps control how strongly hemoglobin holds onto oxygen
A right shift of the hemoglobin-oxygen curve means:
A. Increased oxygen affinity
B. Decreased oxygen affinity
C. No oxygen release
D. Increased hemoglobin production
B. decreased oxygen affinity
41. A right shift causes hemoglobin to:
A. Hold oxygen more tightly
B. Release oxygen more easily
C. Stop carrying oxygen
D. Become bilirubin
B. release oxygen more easily.
Because hemoglobin holds oxygen less tightly during a right shift, it releases more oxygen.
42. A right shift results in:
A. Increased oxygen delivery to tissues
B. Decreased oxygen delivery to tissues
C. No oxygen delivery
D. Increased iron storage
A. increased oxygen delivery to tissues.
More oxygen is released from hemoglobin, so the tissues receive more O₂
43. A left shift means hemoglobin has:
A. Decreased oxygen affinity
B. Increased oxygen affinity
C. No affinity for oxygen
D. Increased bilirubin
B. increased oxygen affinity.
A left shift means hemoglobin holds oxygen more tightly
44. A left shift results in:
A. Increased oxygen delivery to tissues
B. Decreased oxygen delivery to tissues
C. Increased CO₂ production
D. Increased RBC lifespan
B. Decreased oxygen delivery to tissues
If hemoglobin holds oxygen too tightly, it doesn't release as much oxygen to the tissues
anemia causes a shift to the:
A. Left B. Right C. Center D. No shift
B. right shift
bc we have low blood we need more blood and oxygen released to the tissues. anemia causes a right shift, helping release oxygen to the tissues.
Which protein transports iron in the blood?
A. Ferritin B. Transferrin C. Spectrin D. Glycophorin
B. Transferrin
47. Iron is transported to developing RBCs primarily as:
A. Fe⁺ B. Fe²⁺ C. Fe³⁺ D. Ca²⁺
C. Fe³⁺ (ferric iron)
48. Fe³⁺ is also called:
A. Ferrous
B. Ferric
C. Ferritin
D. Ferroglobin
B. Ferric iron
49. Fe²⁺ is also called:
A. Ferric B. Ferrous C. Ferritin D. Transferrin
B. Ferrous
Fe²⁺ = ferrous iron.
50. Fe³⁺ entering the developing RBC is reduced to:
A. Fe⁺ B. Fe²⁺ C. Fe⁴⁺ D. Ca²⁺
B. Fe²⁺
Inside the developing RBC, Fe³⁺ is reduced to Fe²⁺, which is needed for heme formation
51. Where does Fe³⁺ go to be reduced to Fe²⁺?
A. Nucleus B. Mitochondria C. Golgi apparatus D. Cell membrane
B. Mitochondria
The developing RBC's mitochondria are involved in converting Fe³⁺ to Fe²⁺.
52. Fe²⁺ is inserted into the:
A. Globin chain
B. Protoporphyrin ring
C. Cholesterol molecule
D. Albumin molecule
B. Protoporphyrin ring
Fe²⁺ is inserted into the protoporphyrin ring to make heme
53. Protoporphyrin + Fe²⁺ produces:
A. Bilirubin B. Heme C. Ferritin D. Transferrin
B. Heme
54. Excess iron inside the cell is stored as:
A. Albumin B. Ferritin C. Bilirubin D. Spectrin
B. Ferritin
55. If protoporphyrin synthesis is impaired, iron can accumulate around the:
A. Cell membrane
B. Nucleus
C. Mitochondrial membrane only
D. Golgi
B. Nucleus
When protoporphyrin synthesis is defective, iron can accumulate around the nucleus
A developing RBC with a ring of iron around its nucleus is called a:
A. Target cell
B. Spherocyte
C. Ringed sideroblast
D. Acanthocyte
C. Ringed sideroblast
57. Which stain is used to demonstrate iron in ringed sideroblasts?
A. Wright stain
B. Prussian blue
C. Gram stain
D. PAS stain
B. Prussian Blue
Prussian blue stain is used to show iron deposits in cells