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Oxygen Hemoglobin Dissociation
Curve
R.Srihari
• Introduction
• Hemoglobin
• The Curve
• P50
• Summary
Introduction
• The oxygen–hemoglobin dissociation
curve plots the proportion of hemoglobin in
its saturated form on the vertical axis against
the prevailing oxygen tension on the
horizontal axis
• Important tool for understanding how blood
carries and releases oxygen
• More specifically it relates between the
– Percentage of Oxygen carrying capacity of
Haemoglobin and Partial pressure of Oxygen
Hemoglobin
• Heme + Globin – Quarternary
– Heme: present as 4 subunits connected by
polypeptide globin chains as 2 alpha and 2 beta
units(adult)
• Each Heme contains one atom of ferrous iron
Each ferrous iron has ability of binding reversibly to one
oxygen molecule (via Oxygenation reaction)
• Hb in 2 forms –deoxyHb and oxyHb
– In DeoxyHb- globin units are tightly bound(TENSE
CONFIGURATION) –which has reduces affinity of
Hb molecule to Oxygen
When 1st oxygen is bound- the bonds holding globin
chains are released producing RELAXED
CONFIGURATION
Which exposes more oxygen binding sites leading to
high fold affinity to oxygen binding.
The Curve
• The 'plateau' portion of the
curve is the range that exists
at the pulmonary capillaries
(minimal reduction of oxygen
transported until the p(O2)
falls 50 mmHg).
• The 'steep' portion of the
curve is the range that exists
at the systemic capillaries (a
small drop in systemic capillary
p(O2) can result in the release
of large amounts of oxygen for
the metabolically active cells).
• At pressures above about 60 mmHg, the standard
dissociation curve is relatively flat, which means that
the oxygen content of the blood does not change
significantly even with large increases in the oxygen
partial pressure
• Although binding of oxygen to hemoglobin continues
to some extent for pressures about 50 mmHg, as
oxygen partial pressures decrease in this steep area of
the curve,. the oxygen is unloaded to peripheral tissue
readily as the hemoglobin's affinity diminishes. The
partial pressure of oxygen in the blood at which the
hemoglobin is 50% saturated, typically about 26.6
mmHg for a healthy person, is known as the P50
P50
• P50 is a conventional measure of hemoglobin
affinity for oxygen
• In the presence of disease or other conditions
that change the hemoglobin's oxygen affinity
and, consequently, shift the curve to the right
or left, the P50 changes accordingly
• Increased P50 indicates a rightward shift of
the standard curve, which means that a larger
partial pressure is necessary to maintain a
50% oxygen saturation. This indicates a
decreased affinity
• Conversely, a lower P50 indicates a leftward
shift and a higher affinity.
• SHIFT TO THE LEFT
– AS IN PULMONARY
CAPILLARIES
HIGH pH
DECREASED TEMP.
DECREASED CO2
FETAL HB
METHAEMOGLOBINEMIA
• INCREASED AFFINITY OF HB
TO OXYGEN –LESS RELEASE
OF OXYGEN
• SHIFT TO THE RIGHT
– AS IN PLACENTA AND
MUSCLES
HIGH Ph
INCREASED TEMP.
INCREASED CO2
INCREASED 2,3 DPG
• DECREASED AFFINITY OF
HB TO OXYGEN- MORE
RELEASE OF OXYGEN
FROM HB
O
X
Y
G
E
N
-
H
B
C
U
R
V
E
THANK YOU

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  • 2. • Introduction • Hemoglobin • The Curve • P50 • Summary
  • 3. Introduction • The oxygen–hemoglobin dissociation curve plots the proportion of hemoglobin in its saturated form on the vertical axis against the prevailing oxygen tension on the horizontal axis • Important tool for understanding how blood carries and releases oxygen
  • 4. • More specifically it relates between the – Percentage of Oxygen carrying capacity of Haemoglobin and Partial pressure of Oxygen
  • 5. Hemoglobin • Heme + Globin – Quarternary – Heme: present as 4 subunits connected by polypeptide globin chains as 2 alpha and 2 beta units(adult) • Each Heme contains one atom of ferrous iron Each ferrous iron has ability of binding reversibly to one oxygen molecule (via Oxygenation reaction)
  • 6.
  • 7. • Hb in 2 forms –deoxyHb and oxyHb – In DeoxyHb- globin units are tightly bound(TENSE CONFIGURATION) –which has reduces affinity of Hb molecule to Oxygen When 1st oxygen is bound- the bonds holding globin chains are released producing RELAXED CONFIGURATION Which exposes more oxygen binding sites leading to high fold affinity to oxygen binding.
  • 8. The Curve • The 'plateau' portion of the curve is the range that exists at the pulmonary capillaries (minimal reduction of oxygen transported until the p(O2) falls 50 mmHg). • The 'steep' portion of the curve is the range that exists at the systemic capillaries (a small drop in systemic capillary p(O2) can result in the release of large amounts of oxygen for the metabolically active cells).
  • 9. • At pressures above about 60 mmHg, the standard dissociation curve is relatively flat, which means that the oxygen content of the blood does not change significantly even with large increases in the oxygen partial pressure • Although binding of oxygen to hemoglobin continues to some extent for pressures about 50 mmHg, as oxygen partial pressures decrease in this steep area of the curve,. the oxygen is unloaded to peripheral tissue readily as the hemoglobin's affinity diminishes. The partial pressure of oxygen in the blood at which the hemoglobin is 50% saturated, typically about 26.6 mmHg for a healthy person, is known as the P50
  • 10. P50 • P50 is a conventional measure of hemoglobin affinity for oxygen • In the presence of disease or other conditions that change the hemoglobin's oxygen affinity and, consequently, shift the curve to the right or left, the P50 changes accordingly
  • 11. • Increased P50 indicates a rightward shift of the standard curve, which means that a larger partial pressure is necessary to maintain a 50% oxygen saturation. This indicates a decreased affinity • Conversely, a lower P50 indicates a leftward shift and a higher affinity.
  • 12. • SHIFT TO THE LEFT – AS IN PULMONARY CAPILLARIES HIGH pH DECREASED TEMP. DECREASED CO2 FETAL HB METHAEMOGLOBINEMIA • INCREASED AFFINITY OF HB TO OXYGEN –LESS RELEASE OF OXYGEN • SHIFT TO THE RIGHT – AS IN PLACENTA AND MUSCLES HIGH Ph INCREASED TEMP. INCREASED CO2 INCREASED 2,3 DPG • DECREASED AFFINITY OF HB TO OXYGEN- MORE RELEASE OF OXYGEN FROM HB O X Y G E N - H B C U R V E