You are on page 1of 3

How Are Oxygen and Carbon Dioxide Transported in Blood?

CONCEPT : Blood is a connective tissue that consists of cells in a

watery extracellular matrix. Besides carrying oxygen and
carbon dioxide between cells and the lungs, blood transports
nutrients from the digestive tract to other tissues in the body,
moves waste products to the kidney and liver for processing,
conveys hormones from glands to target tissues, delivers
immune system cells to sites of infection, and distributes heat
throughout the body.
CONCEPT : Oxygen Molecule is Non Polar, so solubility in blood plasma
less. Then how is Oxygen Transported in Blood?
Hemoglobin (a protein molecule) combines reversibly with up to 4 O2
molecules and increases the capacity of blood to transport O2 by about 60fold, making high levels of metabolism in higher animals possible.

So, Transport of Oxygen

97 % RBCs
3 % dissolved state in the plasma.

Hemoglobin picks up O2 where PO2 is high and release it where PO2 is lower.

CONCEPT : Oxygen

Delivery by Hemoglobin Is Extremely
Efficient due to cooperative binding and the Bohr shift.

O2 saturation (%) of hemoglobin

Cooperative binding is important because it makes hemoglobin
exquisitely sensitive to changes in the of values of PO2 in tissues.
% O2 changes


In this part of the graph, a
small change in PO leads to
a large change in how much
O2 unloads from hemoglobin

% O2







PO2 (mm Hg) in blood within tissue
FIGURE 45.14 The Oxygen–Hemoglobin Equilibrium Curve Is
Sigmoidal. A sigmoidal curve has three distinct regions.


or S-shaped.The most remarkable feature of the oxygen–hemoglobin equilibrium curve is that it is sigmoidal. 100 Resting 80 Exercising e iv at r pe oo c on N 60 40 20 0 0 20 30 ng di n bi 40 60 80 PO2 (mm Hg) in blood within tissue 100 . large amounts of O2 are delivered to resting and exercising tissues. 0 20 30 40 60 80 100 PO2 (mm Hg) in blood within tissue O2 saturation (%) of hemoglobin (b) Without cooperative binding. the loss of a bound oxygen molecule changes hemoglobin’s conformation in a way that makes the loss of additional oxygen molecules more likely. 100 80 Resting 40 Exercising er op Co 20 0 ind i ng 60 at ive b O2 saturation (%) of hemoglobin (a) With cooperative binding. The pattern occurs because the binding of each successive oxygen molecule to a subunit of the hemoglobin molecule causes a conformational change in the protein that makes the remaining subunits much more likely to bind oxygen. smaller amounts of O2 would be delivered to resting and exercising tissues. Conversely.

As pH drops. As FIGURE 45. O2 saturation (%) of hemoglobin As noted above. As a result. which dissociates and releases a hydrogen ion. The CO2 produced by exercising muscle reacts with the water in blood to form carbonic acid.16 The Bohr Shift Makes Hemoglobin More Likely to Release Oxygen to Tissues with Low pH.4 80 60 pH 7. Decreases in pH alter hemoglobin’s conformation. The Bohr shift is important because it makes hemoglobin more likely to release oxygen during exercise or other conditions in which PCO2 is high. representing a greater unloading of oxygen to tissues at any given PO2. Increasing temperature has the same result: It shifts the curve to the right. These shape changes make hemoglobin more likely to unload O2 at any given value of tissue PO2.Sub Concept : Hemoglobin—like other proteins—is sensitive to changes in pH and temperature. oxygen becomes less likely to stay bound to hemoglobin at all values of tissue PO2. this phenomenon. Exercising tissues have lower pH than resting tissues and thus receive more oxygen from hemoglobin. causes the oxygen–hemoglobin equilibrium curve to shift to the right when pH declines.16 shows. pH is low. the temperature and partial pressure of CO2 rise in active muscle tissue during exercise. and tissues are under oxygen stress.2 Bohr shift 40 20 0 0 20 30 40 60 80 100 PO2 (mm Hg) in blood within tissue FIGURE 45. . 100 pH 7. known as the Bohr shift. the pH of the blood in exercising muscle drops.