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(Structure, Oxygen & CO₂ Transport, Oxygen Dissociation Curve)
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Hemoglobin (Hb) is a tetrameric protein.
Consists of 4 globin chains + 4 heme groups.
Each heme contains protoporphyrin IX + Fe²⁺.
One molecule of Hb binds 4 O₂ molecules.
HbA (α₂β₂) — main adult Hb (~97%).
HbA₂ (α₂δ₂) — ~2%.
HbF (α₂γ₂) — <1% in adults; predominant in fetus.
Globin is a protein with helical regions.
Each chain surrounds one heme pocket.
Fe²⁺ is held by:
Proximal histidine (F8)
Distal histidine (E7) helps binding O₂.
Hb has two αβ dimers.
Exists in two states:
T-state (Tense): low O₂ affinity
R-state (Relaxed): high O₂ affinity
Binding of O₂ shifts Hb → T → R transition (cooperative binding).
Each Hb carries 4 O₂ molecules (one per heme iron).
Hb carries 98% of total oxygen; plasma carries 2%.
O₂ binds reversibly to Fe²⁺ without oxidation.
Fe²⁺ remains in reduced state (oxyhemoglobin is NOT Fe³⁺).
↓ pH (acidic)
↑ CO₂
↑ Temperature
↑ 2,3-BPG
→ Shift O₂ curve to the right (↓ affinity, ↑ release).
CO₂ is transported in three forms:
CO₂ + H₂O → H₂CO₃ → H⁺ + HCO₃⁻
Enzyme: Carbonic anhydrase (RBC cytosol).
CO₂ binds to terminal amino groups of globin chains (not heme).
Deoxygenated Hb carries more CO₂ (Haldane effect).
Directly dissolved in plasma.
The ODC is sigmoid due to cooperative binding of oxygen.
Memory: CADET → right shift
CO₂ ↑
Acid ↑ (↓ pH)
DPG ↑ (2,3-BPG)
Exercise ↑
Temperature ↑
Seen in:
Exercise
Anemia
High altitude
Fever
Acidosis (DKA, sepsis)
↓ 2,3-BPG
↓ Temperature
↓ CO₂
↑ pH (alkalosis)
HbF (fetal hemoglobin)
CO poisoning
Methemoglobinemia
Left shift means less O₂ delivered to tissues.
P50 = PO₂ at which Hb is 50% saturated.
Normal P50 ≈ 26 mmHg.
Right shift: ↑ P50
Left shift: ↓ P50
Structure: α₂γ₂
Higher O₂ affinity due to low 2,3-BPG binding.
Facilitates transfer of O₂ from mother to fetus.
Curve is shifted left.
Myoglobin = monomer, hyperbolic curve, no cooperativity.
Has higher O₂ affinity than Hb.
Acts as O₂ reservoir in muscle.
Hemoglobin is an allosteric protein, meaning its activity changes when molecules bind at sites other than the oxygen-binding site.
Binding of the first O₂ increases the affinity for the next O₂.
Called positive cooperativity.
Responsible for the sigmoid shape of the O₂ dissociation curve.
Deoxygenated Hb = T-state (tense) → low O₂ affinity.
Oxygenated Hb = R-state (relaxed) → high O₂ affinity.
O₂ binding causes conformational change that breaks salt bridges → R-form.
↑ H⁺ (acidosis) stabilizes T-form → Hb releases more O₂.
This is the Bohr effect.
CO₂ binds to terminal amino groups → carbaminohemoglobin.
Stabilizes T-form → promotes O₂ release (Haldane effect).
2,3-BPG binds between β-chains → stabilizes T-form → ↓ O₂ affinity.
Helps unloading of O₂ in tissues.
2,3-BPG is produced in RBCs via the Rapoport–Luebering shunt.
Binds to the central cavity of deoxygenated Hb.
Binds only to β-chains → therefore:
HbA (α₂β₂) → strongly affected
HbF (α₂γ₂) → weakly affected → higher O₂ affinity
Decreases hemoglobin’s affinity for oxygen.
Shifts the O₂ dissociation curve to the right.
Increases P50 (more O₂ needed for 50% saturation).
Improves O₂ delivery to tissues.
High altitude
Anemia
Hypoxia
Chronic lung disease
Exercise
Hyperthyroidism
Stored blood (banked blood)
Hypothermia
HbF presence (poor binding of 2,3-BPG)
Alkalosis
Isohydric transport refers to CO₂ being carried in blood without altering the pH dramatically, thanks to buffering by hemoglobin.
CO₂ enters RBC.
Combined with water → H₂CO₃ → H⁺ + HCO₃⁻
Catalyzed by carbonic anhydrase.
H⁺ is buffered by deoxygenated hemoglobin.
Hb acts as a buffer → prevents drastic change in pH.
HCO₃⁻ leaves RBC and is carried in plasma.
Allows 70% of CO₂ to be transported as bicarbonate
without making the blood acidic.
Hemoglobin binding of H⁺ is key.
Deoxygenated Hb (in tissues) binds H⁺ better → favors CO₂ transport.
This is part of the Haldane effect.
This is the exchange of bicarbonate and chloride ions between RBCs and plasma to maintain electrical neutrality.
CO₂ diffuses into RBC.
Converts to HCO₃⁻ + H⁺ (carbonic anhydrase).
HCO₃⁻ leaves RBC into plasma.
Cl⁻ enters RBC to maintain charge balance.
➡ RBC becomes chloride-rich in tissues.
CO₂ is expelled from blood.
HCO₃⁻ enters RBC from plasma.
Cl⁻ moves out of RBC to maintain neutrality.
HCO₃⁻ + H⁺ → H₂CO₃ → CO₂ (exhaled).
➡ RBC loses chloride in lungs.
Maintains electrical neutrality.
Enables maximum transport of CO₂ as bicarbonate.
Essential for acid-base homeostasis.
Occurs in all RBCs during CO₂ transport.
HbF = α₂γ₂
γ-chains replace β-chains of adult Hb.
Predominant Hb in fetus and newborn.
Higher affinity for oxygen than HbA.
Curve shifted left.
Because 2,3-BPG binds poorly to γ-chains.
Facilitates O₂ uptake from maternal blood.
Allows fetal RBCs to extract oxygen across the placenta.
Protects fetus from low oxygen tension in utero.
HbF declines rapidly after birth.
Major switch from γ → β chains completed by 6 months.
Adult pattern (HbA) predominates thereafter.
β-thalassemia major
Hereditary persistence of fetal Hb (HPFH)
Sickle cell disease (after hydroxyurea therapy)
(Abnormal chemical forms of hemoglobin)
Hb + O₂
Normal physiologic oxygenated form.
Hb without oxygen.
Found in venous blood.
Hb where iron is Fe³⁺ (ferric).
Cannot bind oxygen.
Hb bound to carbon monoxide (CO).
CO₂ bound to terminal NH₂ groups of globin chains.
Hb with sulfur atom incorporated.
Irreversible.
Seen with sulfur-containing drugs.
MetHb + cyanide ion.
Used in laboratory estimation of Hb.
(A highly important exam topic)
Hemoglobin bound to carbon monoxide.
Hb has 200–250 times higher affinity for CO than for O₂.
CO shifts the O₂ dissociation curve left → reduced O₂ unloading.
Causes tissue hypoxia without anemia.
CO poisoning symptoms:
Headache
Cherry-red skin
Confusion
Seizures
Coma
Pulse oximetry is normal (false reading).
CO-Hb gives blood a bright red color.
Car exhaust
Fire/smoke inhalation
Tobacco smoke
Generators used in closed rooms
100% oxygen
Hyperbaric oxygen (severe cases)
Remove exposure
Hemoglobin with iron oxidized to Fe³⁺ instead of Fe²⁺.
Fe³⁺ cannot bind O₂ → functional anemia.
Drugs/chemicals:
Nitrites
Dapsone
Nitrates
Aniline dyes
Local anesthetics (benzocaine)
Congenital:
Cytochrome b₅ reductase deficiency
Cyanosis with normal PaO₂.
Chocolate-brown colored blood.
Low pulse oximetry readings (85% “methemoglobin saturation plateau”).
Shortness of breath, headache, fatigue.
Co-oximetry (gold standard).
Methemoglobin level measurement.
Methylene blue (reduces Fe³⁺ → Fe²⁺).
Vitamin C (adjunct).
Avoid causative drugs.
| Condition | Iron State | O₂ Binding | Blood Color | O₂ Curve |
|---|---|---|---|---|
| Oxy-Hb | Fe²⁺ | Yes | Bright red | Normal |
| Deoxy-Hb | Fe²⁺ | No O₂ bound | Dark red | Normal |
| Met-Hb | Fe³⁺ | Cannot bind O₂ | Chocolate brown | Left shift |
| CO-Hb | Fe²⁺ + CO | O₂ blocked | Bright red |
Left shift |
Hemoglobin variants are structural abnormalities of globin chains due to single amino acid substitutions or deletions.
HbS (sickle cell hemoglobin) – β6 Glu → Val
HbC – β6 Glu → Lys
HbE – β26 Glu → Lys (common in NE India)
HbD-Punjab – another β-chain variant
Hb M – oxidation of Fe²⁺ → Fe³⁺ (methemoglobinemia)
HbF persistence – Hereditary persistence of fetal Hb (HPFH)
Affect solubility, stability, or oxygen affinity of Hb.
Some variants cause hemolysis, polymerization, or decreased oxygen delivery.
(Most important hemoglobinopathy)
Point mutation in β-globin gene: Valine replaces Glutamic acid at position 6 (Glu → Val).
Produces abnormal HbS.
In low O₂ → HbS polymerizes → forms rigid, sickle-shaped RBCs.
Sickled cells cause:
Hemolysis
Vaso-occlusion
Microinfarcts
Painful crises
Avascular necrosis
Acute chest syndrome
Anemia
Dactylitis in children
Autosplenectomy → Howell–Jolly bodies
Sickle cells on smear
↑ Reticulocytes
↑ Indirect bilirubin
↑ LDH
Positive sickling test
Hydroxyurea → ↑ HbF (reduces sickling)
Blood transfusion
Pain control
Bone marrow transplant (curative)
Genetic disorders causing reduced synthesis of α- or β-globin chains.
Gene deletion of α-globin genes (4 total).
1 gene deleted → Silent carrier
2 deleted → α-thalassemia trait
3 deleted → HbH disease (β₄ tetramers)
4 deleted → Hydrops fetalis (Hb Bart’s; γ₄) → fatal
Mutations causing decreased β-chain production.
β⁺ (partial reduction)
β⁰ (complete absence)
Mild anemia
Very high HbA₂ (>3.5%)
Severe microcytic anemia
Extramedullary hematopoiesis → chipmunk facies
Splenomegaly
High HbF levels
Iron overload from transfusions
Regular transfusions
Iron chelation (deferoxamine)
Bone marrow transplant (curative)
Monomer (single polypeptide).
Contains one heme group → binds one O₂.
Very high O₂ affinity.
No cooperativity (hyperbolic curve).
Acts as an oxygen reservoir in muscle.
Myoglobinuria seen in:
Rhabdomyolysis
Crush injuries
Severe muscle damage
Causes dark red/brown urine.
Can precipitate in kidneys → acute renal failure.
(From the hemoglobin perspective)
Reduced oxygen-carrying capacity of blood.
Premature RBC destruction.
Causes: HbS, HbC, G6PD deficiency, thalassemia, autoimmune.
Features:
↑ unconjugated bilirubin
↑ LDH
↓ haptoglobin
Reticulocytosis
Reduced Hb synthesis → small, pale RBCs.
Causes:
Iron deficiency
Thalassemias
Sideroblastic anemia
Chronic disease
Acute blood loss
Hemolysis
Chronic kidney disease (↓ EPO)
Vitamin B12 or folate deficiency
Alcoholism
Liver disease
Reticulocytosis
| Feature | HbS | Thalassemia | Myoglobin |
|---|---|---|---|
| Defect | Structural mutation | Reduced synthesis | Structural monomer |
| O₂ Affinity | Low | Normal/high | Very high |
| Curve | Right-shift & polymerization | Affected by chain imbalance | Hyperbolic |
| Clinical | Pain crises, hemolysis | Microcytosis, marrow expansion |
Muscle oxygen store |
Hb is a tetramer: α₂β₂ in adults.
Each chain contains a heme group with Fe²⁺.
Fe²⁺ binds O₂; Fe³⁺ cannot.
Exists in two states:
T-state (tense, low O₂ affinity)
R-state (relaxed, high O₂ affinity)
Hb carries 98% of oxygen in blood.
O₂ binding is cooperative → sigmoid O₂ dissociation curve.
Exchange of one O₂ changes affinity of other subunits.
Sigmoid shape due to cooperative binding.
Right shift (↓ affinity, ↑ O₂ release):
↑ CO₂, ↑ H⁺ (↓ pH), ↑ Temperature, ↑ 2,3-BPG, Exercise.
Left shift (↑ affinity):
HbF, CO-Hb, Met-Hb, ↓ CO₂, ↓ Temperature, ↓ 2,3-BPG.
P50 = 26 mmHg; increased by right shift.
↑ CO₂ or ↓ pH → Hb releases O₂ (right shift).
Helps oxygen delivery to tissues.
Deoxygenated Hb binds more CO₂ and H⁺.
Oxygenated Hb releases CO₂.
Important for CO₂ unloading in lungs.
Produced in RBCs via Rapoport–Luebering shunt.
Binds to β-chains → stabilizes T-state → ↓ O₂ affinity.
↑ in high altitude, hypoxia, anemia, exercise.
↓ in stored blood, alkalosis, HbF presence (γ-chains do not bind it).
CO₂ + H₂O → H₂CO₃ → H⁺ + HCO₃⁻ (carbonic anhydrase).
H⁺ buffered by deoxygenated Hb → prevents acidosis.
Allows 70% of CO₂ transport as bicarbonate.
At tissues: HCO₃⁻ leaves RBC → Cl⁻ enters (forward shift).
At lungs: HCO₃⁻ enters RBC → Cl⁻ exits (reverse shift).
Maintains electrical neutrality.
Structure: α₂γ₂.
Binds O₂ more strongly (left shift).
Poor interaction with 2,3-BPG.
High levels in fetus → facilitates placental oxygen transfer.
↑ in HPFH, β-thalassemia, hydroxyurea therapy.
Oxyhemoglobin: normal oxygenated form.
Deoxyhemoglobin: venous blood.
Carboxyhemoglobin: Hb + CO (bright red).
Methemoglobin: Fe³⁺ form, cannot bind O₂.
Carbaminohemoglobin: Hb + CO₂ (globin binding).
Sulfhemoglobin: irreversible sulfur binding.
CO binds Hb 200–250 times more strongly than O₂.
Causes tissue hypoxia despite normal PaO₂.
Pulse oximeter is falsely normal.
Treat with 100% oxygen or hyperbaric O₂.
Seen in smoke inhalation, exhaust exposure, smoking.
Iron is oxidized to Fe³⁺ → cannot bind O₂.
Blood becomes chocolate brown.
Causes: nitrates, nitrites, dapsone, benzocaine.
Treated with methylene blue.
Structural changes in globin chains.
Examples: HbS, HbC, HbE, HbD-Punjab, HbM.
May affect solubility, stability, or O₂ affinity.
Mutation: β6 Glu → Val.
Polymerizes in low O₂ → sickling.
Causes hemolysis, vaso-occlusion, pain crises.
HbF reduces sickling → hydroxyurea benefits.
Spleen becomes auto-infarcted → Howell–Jolly bodies.
↓ Synthesis of α- or β-globin chains.
One gene deletion → silent carrier.
Four deletions → Hb Bart’s → hydrops fetalis (fatal).
↓ β-chain synthesis.
Major: severe anemia, crew-cut skull, hepatosplenomegaly, ↑ HbF.
Minor: mild anemia, ↑ HbA₂ (>3.5%).
Monomeric, one heme group.
Very high O₂ affinity (hyperbolic curve).
O₂ storage protein in muscle.
Elevated in rhabdomyolysis → myoglobinuria → renal damage.
Hemolytic anemia: HbS, G6PD deficiency, thalassemia.
Microcytic anemia: iron deficiency, β-thalassemia, chronic disease.
Normocytic anemia: acute blood loss, CKD.
Macrocytic anemia: B12/folate deficiency.
HbA = α₂β₂; HbF = α₂γ₂ (left shift).
P50 = 26 mmHg.
CO binds Hb 200–250× stronger than O₂.
Met-Hb = Fe³⁺; treat with methylene blue.
Right shift = CADET ↑ (CO₂, Acid, DPG, Exercise, Temp).
HbS = Glu → Val (β6).
β-thalassemia major → ↑ HbF, skeletal deformities.
Chloride shift = HCO₃⁻ ↔ Cl⁻ exchange.
Myoglobin = monomer, hyperbolic curve, high affinity.
A. α₂γ₂
B. α₂δ₂
C. α₂β₂
D. β₄
Answer: C
A. Ferric state
B. Ferrous state
C. Elemental state
D. Ferritin-bound state
Answer: B
A. Bohr effect
B. Haldane effect
C. Cooperative binding of oxygen
D. Binding of CO₂
Answer: C
A. Increased affinity for oxygen
B. Left shift of curve
C. Reduced tissue oxygenation
D. Reduced affinity → increased O₂ delivery to tissues
Answer: D
A. Low temperature
B. High pH
C. Low 2,3-BPG
D. High CO₂
Answer: D
A. Affinity for O₂ is increased
B. Affinity for O₂ is decreased
C. HbF is dominant
D. CO is bound
Answer: B
A. Heme iron
B. α-chains
C. β-chains in the central cavity
D. γ-chains
Answer: C
A. HbA
B. HbA₂
C. HbF
D. Methemoglobin
Answer: C
A. CO bound to hemoglobin
B. Shifting of chloride across RBC membrane
C. CO₂ dissolved in plasma
D. CO₂ transport as HCO₃⁻ while H⁺ is buffered by hemoglobin
Answer: D
A. Chloride leaving RBC
B. Chloride entering RBC
C. Potassium entering RBC
D. CO₂ entering plasma
Answer: B
A. It has more α-chains
B. It has more iron
C. It binds poorly to 2,3-BPG
D. It contains ferric iron
Answer: C
A. Oxyhemoglobin
B. Deoxyhemoglobin
C. Carboxyhemoglobin
D. Methemoglobin (Fe³⁺)
Answer: D
A. Nitrite exposure
B. Iron deficiency
C. Carbon monoxide exposure
D. ATP depletion in RBCs
Answer: C
A. Right
B. Left
C. Flat
D. Hyperbolic
Answer: B
A. β26 Glu → Lys
B. β6 Glu → Val
C. β6 Glu → Asp
D. α1 deletion
Answer: B
A. High oxygen tension
B. Cold exposure only
C. Low oxygen tension
D. High HbF
Answer: C
A. Heme synthesis
B. Iron absorption
C. Globin chain synthesis
D. Chloride transport
Answer: C
A. High HbA₂
B. Normal HbF
C. Markedly increased HbF
D. High 2,3-BPG deficiency
Answer: C
A. HbH disease
B. HbC disease
C. Hydrops fetalis (Hb Bart’s)
D. Mild anemia
Answer: C
A. It has 4 heme groups
B. It is a tetramer
C. It has a hyperbolic O₂ curve
D. It has lower affinity for oxygen
Answer: C
A. Malaria
B. Iron deficiency
C. Rhabdomyolysis
D. Pneumonia
Answer: C
A. Carboxyhemoglobin
B. Anemia
C. Methemoglobinemia
D. HbE disease
Answer: C
A. Hydroxyurea
B. Blood transfusion
C. Iron therapy
D. Methylene blue
Answer: D
A. Falls to zero
B. Shows high CO₂
C. May remain falsely normal
D. Shows low pH
Answer: C
A. HbS
B. HbC
C. β-Thalassemia major
D. HbE trait
Answer: C
Diagnosis: Sickle cell disease
Mechanism: β6 Glu → Val mutation → polymerization of HbS in low O₂
Why high HbF helps: HbF inhibits sickling
Diagnosis: β-Thalassemia major
Mechanism: Absent β-chains → excess α-chains → ineffective erythropoiesis
Diagnosis: α-Thalassemia — deletion of all four α-genes
Mechanism: No α-chains → Hb Bart’s has extremely high O₂ affinity → no O₂ delivery
Diagnosis: Physiological adaptation to high altitude
Mechanism: 2,3-BPG ↑ → right shift → enhanced O₂ release
Diagnosis: CO poisoning (Carboxyhemoglobin)
Mechanism: CO binds Hb 250× stronger than O₂ → tissue hypoxia
Treatment: 100% O₂ or hyperbaric O₂
Diagnosis: Methemoglobinemia (Fe³⁺ state)
Mechanism: Oxidation of Fe²⁺ → Fe³⁺
Treatment: Methylene blue
Diagnosis: Congenital methemoglobinemia
Mechanism: Cytochrome b₅ reductase deficiency
Diagnosis: Tissue hypoxia due to infection
Mechanism: Fever + acidosis → ↓ O₂ affinity → better tissue delivery
Diagnosis: Chronic CO₂ retention
Mechanism: CO₂ binding to amino terminals of globin chains
Relevance: Haldane effect → deoxygenated Hb binds more CO₂
Diagnosis: Benzocaine-induced methemoglobinemia
Reason: Fe³⁺ cannot bind oxygen
Treatment: Methylene blue
Diagnosis: β-Thalassemia minor
Mechanism: Reduced β-chain synthesis → compensatory ↑ HbA₂
Diagnosis: Myoglobinuria due to rhabdomyolysis
Mechanism: Myoglobin released from muscle → renal toxicity
Diagnosis: Physiological adaptation
Mechanism: Myoglobin acts as muscle O₂ reservoir
Diagnosis: CO exposure from cigarettes
Result: Tissue hypoxia despite normal Hb
Long-term risk: Polycythemia (compensatory)
Diagnosis: Dilutional/acute blood loss anemia
Mechanism: RBCs normal size; loss due to hemorrhage
Diagnosis: High fetal hemoglobin level
Mechanism: HbF has high O₂ affinity → less O₂ released to tissues
Diagnosis: Methemoglobinemia
Mechanism: Oxidation of Fe²⁺ → Fe³⁺
Best test: Co-oximetry
Diagnosis: Hemolytic anemia
Mechanism: Hb breakdown → ↑ unconjugated bilirubin
Diagnosis: HbE disease
Mechanism: β26 Glu → Lys mutation
Prevalent in: Assam, Bengal, Thailand
Diagnosis: Methemoglobinemia
Clue: Saturation plateau at 85% is diagnostic
A tetramer of two α and two β chains, each containing a heme group with Fe²⁺.
Only Fe²⁺ can bind oxygen; Fe³⁺ cannot.
Reversible coordination bond between O₂ and Fe²⁺ in heme.
Tense state → low oxygen affinity.
Relaxed state → high oxygen affinity.
Cooperative binding of oxygen.
PO₂ at which Hb is 50% saturated; normal ~26 mmHg.
Decreased oxygen affinity (right shift).
↑ CO₂, ↑ H⁺, ↑ Temperature, ↑ 2,3-BPG.
H⁺ and CO₂ decrease Hb’s O₂ affinity → O₂ release in tissues.
Oxygenated blood carries less CO₂; deoxygenated blood carries more.
Binds β-chains → stabilizes T-state → reduces O₂ affinity.
HbF (α₂γ₂) binds 2,3-BPG weakly → O₂ affinity rises → left shift.
Pathway in RBCs producing 2,3-BPG.
CO₂ bound to terminal amino groups of globin chains.
Transport of CO₂ as HCO₃⁻ while H⁺ is buffered by Hb.
Exchange of HCO₃⁻ and Cl⁻ across RBC membrane for neutrality.
Protects against sickling → increased by hydroxyurea in sickle cell disease.
Oxy-Hb, Deoxy-Hb, Carboxy-Hb, Met-Hb, Sulf-Hb, Carbamino-Hb.
Hb combined with carbon monoxide.
CO binds Hb 200–250× stronger than O₂ → severe tissue hypoxia.
100% oxygen or hyperbaric oxygen.
Hemoglobin with iron in Fe³⁺ state → cannot bind oxygen.
Nitrates, nitrites, benzocaine, dapsone, aniline dyes.
Chocolate-brown.
Methylene blue.
β6 Glutamic acid → Valine.
HbS polymerizes in low O₂, forming rigid fibers.
High levels of HbF.
Nuclear remnants seen after autosplenectomy in sickle cell.
Reduced synthesis of α- or β-globin chains.
HbA₂ (>3.5%).
β₄ tetramers seen in α-thalassemia (3 gene deletion).
Hb Bart’s (γ₄) → causes hydrops fetalis.
Compensation due to absent β-chains.
Myoglobin is monomeric, binds one O₂, and has hyperbolic curve.
Myoglobin in urine after muscle damage (rhabdomyolysis).
Microcytic hypochromic anemia.
Stored RBCs have low 2,3-BPG → left shift.
Methemoglobin (Fe³⁺).
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