Oxygen transport
Dr. Phoebe Bacalso-Letaba
Oxygen transport
Blood carries oxygen in 2 forms
• A small amount of O2 exists in a simple physical
solution dissolved in the plasma and erythrocyte
intracellular fluid
• Most O2 is carried in a reversible chemical
combination with hemoglobin (Hb) inside the RBC
Dissolved oxygen
• By applying Henry’s law, the amount of dissolved O2 in
the blood (at 37oC) can be computed with the following
simple formula:
Dissolved O2 (ml dl) = PO2 (mm Hg)x0.003
Chemically combined
oxygen
(oxyhemoglobin)
Chemically combined oxygen (oxyhemoglobin)
• As shown in Figure 12-7, each heme complex
contains a centrally located ferrous iron ion.
When Hb is not carrying O2, this ion has four
unpaired electrons. In this deoxygenated state,
the molecule exhibits the characteristics of a
weak acid. Deoxygenated Hb serves as an
important blood buffer for H+, a crucial factor in
CO2 transport.
• When fully saturated, 4 O2 molecules bind to
the iron ion of Hb, one for each protein chain.
With complete O2 binding, all electrons become
paired, and Hb is converted to its oxygenated
state (oxyhemoglobin [HbO2]).
Hemoglobin saturation
• Saturation is a measure of the proportion of available Hb that is carrying
O2. Saturation is computed as the ratio of HbO2 (content) to total Hb
(capacity). Hb arterial O2 saturation (SaO2) is usually expressed as a
percentage of this ratio and calculated according to the following formula:
SaO2 = (HbO2 ÷ Total Hb)x100
• where HbO2 equals the oxyhemoglobin content. If there were a total of 15
g/dL Hb in the blood, of which 7.5 g was HbO2, the SaO2 would be
calculated as follows:
SaO2 (%) = (7.5÷15)x100 = 50%
• In this example, Hb is said to be 50% saturated: Only half of the available
Hb is carrying O2, and the remainder is unoxygenated. In clinical practice,
both SaO2 and total Hb content are measured directly to derive the HbO2.
Normal SaO2 is 95% to 100% depending on the age of the patient.
Total oxygen content of the blood
• Total O2 content of the blood equals the sum of O2 dissolved
and chemically combined with Hb.2,7
• For total O2 content to be calculated, the following three
values must be known:
– (1) PO2
– (2) total Hb content (g/dL), and
– (3) Hb saturation
Total oxygen content of the blood
CaO2 = (0.003xPaO2)+(1.34 x Hb x SaO2)
where:
• CaO2 = Total O2 content (ml/dl)
• PaO2 = Partial pressure of O2 in the blood
• Hb = Hb content (in g/dl)
• SaO2 = Hb saturation with O2 (as a decimal)
Oxyhemoglobin dissociation curve
• Hb saturation with O2 varies with changes in PO2.
• Plotting the saturation (y-axis) against PO2 (x-axis) yields the
HbO2 dissociation curve
• In contrast to dissolved O2, Hb saturation is not linearly related
to PO2. Instead, the relationship forms an S-shaped curve. The
flat upper part of this curve represents the normal operating
range for arterial blood.
Oxyhemoglobin
dissociation
curve
Oxyhemoglobin
dissociation
curve
Relating Hemoglobin Saturation and PaO2
Factors affecting
oxygen loading and
unloading
Bohr Effect-The
impact of changes
in blood pH on Hb
affinity for O2
Low pH (acidity) High pH
shifts the curve to (alkalinity) shifts it
the right to the left.
pH (BOHR EFFECT)
Bohr effect
• Low pH (acidity)
shifts the curve to
the right
• High pH (alkalinity)
shifts it to the left.
Body temperature
Decrease in body Increase in body
temperature - shifts temperature – shifts
the curve to the left, the curve to the right,
increasing Hb affinity and the affinity of Hb
for O2 for O2 decreases
Organic Phosphates
(2,3-Diphosphoglycerate)
Increased 2,3-DPG Decreased 2,3-DPG
concentrations shift concentrations shift
the HbO2 curve to the the curve to the left,
right, promoting O2 increasing Hb affinity
unloading for O2
Abnormal hemoglobin
• Sickle cell hemoglobin (HbS) – is less soluble than
normal Hb, which causes it to become susceptible to
polymerization and precipitation when deoxygenated
• Certain events such as dehydration, hypoxia, and
acidosis cause HbS to crystallize and the RBC to become
hardened and curved like a sickle
Abnormal hemoglobin
Sickle cell hemoglobin (HbS) –
• Erythrocyte Fragility-hemolysis
• Acute Chest Syndrome
• Normal RBC: biconcave
Abnormal hemoglobin
• Methemoglobin (metHb) – is an abnormal form of the
molecule, in which the heme-complex normal Fe++ loses an
electron and is oxidized to its ferric state (Fe++). In the ferric
state, the iron ion cannot combine with O2-
Methemoglobinemia
• As with HbCO, clinical abnormalities come from the
associated increased affinity for O2 and loss of O2-binding
capacity
Abnormal hemoglobin
• Carboxyhemoglobin (HbCo) – is the chemical combination of
Hb with CO. The affinity of Hb for CO is more than 200 times
greater than it is for O2
• Extremely low concentrations of CO can quickly displace O2
from Hb, forming HbCO.
Abnormal hemoglobin
• Fetal hemoglobin (HbF) – fetal life and for up to 1 year
after birth
• HbF has a greater affinity for O2 than normal adult Hb,
manifested by a leftward shift of the HbO2 curve.
Carbon Dioxide
Dissociation Curve
Haldane Effect
• Deoxygenation of
the blood increases
its ability to
carry carbon dioxide
Abnormalities of gas
exchange and transport
Impaired oxygen delivery
O2 delivery (DO2) to the tissues is a product of
arterial O2 content (CaO2) and cardiac output (CO)
• DO2=CaO2 x CO
Hypoxia – when O2 delivery is inadequate for
cellular needs
Hypoxemia
Decreased Partial Pressure of Oxygen in Arterial Blood
• low ambient PO2, hypoventilation,
• impaired diffusion
• V/Q imbalances,
• right-to-left anatomic or physiologic shunting.
PaO2 in older adults may be estimated by using the
following formula:
Expected PaO2 =100 −(0.323 x Age in years)
Hypoxemia
Hemoglobin deficiencies
• Absolute Hb deficiency occurs when the Hb concentration
is lower than normal
• Relative Hb deficiencies are caused by either the
displacement of O2 from normal Hb or the presence of
abnormal Hb variants.
Hypoxemia
Hemoglobin deficiencies
• A low blood Hb concentration may be caused either by a
loss of RBCs, as with hemorrhage, or by inadequate
erythropoiesis (formation of RBCs in the bone marrow).
Reduction in Blood Flow (Shock or Ischemia)
Hypoxia can still occur when the arterial O2 Content
(CaO2) is normal but blood flow is reduced such in:
• Circulatory Failure (Shock)
• Local Reductions in perfusion (Ischemia)
dysoxia
Cyanide poisoning
• cellular uptake of O2 is decreased
• Cyanide disrupts the intracellular cytochrome oxidase
system, preventing cellular use of O2.
Dysoxia also may occur when tissue O2 consumption
becomes dependent on O2 delivery.
Impaired Carbon Dioxide Removal
• Any disorder that decreases alveolar ventilation (VA)
relative to metabolic need impairs CO2 removal.
• Impaired CO2 removal by the lung causes hypercapnia
and respiratory acidosis
Impaired Carbon Dioxide Removal
A decrease in alveolar ventilation occurs when
1. The minute volume is inadequate
2. The dead space ventilation per minute is increased
3. VA / Q imbalance exists
4 Types of Hypoxia:
1. Hypoxemic type – O2 pressure in the blood going to the
tissues is too low to saturate the hemoglobin
2. Anemic type – amount of functional hemoglobin is too small
and hence the capacity of the blood to carry oxygen is too low
4 Types of Hypoxia:
3. Stagnant type – which the blood is or may be normal
but the flow of blood to the tissues is reduced or evenly
distributed
4. Histotoxic type – tissue cells are poisoned and are
therefore unable to make proper use of O2
