Professional Documents
Culture Documents
OXYGEN TRANSPORT
Oxygen Delivery to the Tissues
The O2 delivery system in the body consists of the lungs and
the cardiovascular system. O2 delivery to a particular tissue
depends on the amount of O2 entering the lungs, the
adequacy of pulmonary gas exchange, the blood flow to the
tissue, and the capacity of the blood to carry O2.The blood
flow depends on the degree of constriction of the vascular
bed in the tissue and the cardiac output. The amount of O2 in
the blood is determined by the amount of dissolved O2, the
amount of hemoglobin in the blood, and the affinity of
hemoglobin for O2.
Reaction of hemoglobin and Oxygen
The dynamic of the reaction of the hemoglobin with O2 makes it
particularly suitable O2 carrier.
Hemoglobin is a protein made up of four subunits, each of which
contains a heme moiety attached to a polypeptide chain. In normal
adult, most of the hemoglobin molecules contain two a and two B
chains. Heme is a complex made up of a porphyrin and one atom of
ferrous. Each of the four iron atom, can bind reversibly one O2
molecule. The iron stays in the ferrous state. So the reaction is
oxygenation, not an oxidation.
The quaternary structure of the hemoglobin determines its affinity
for O2. In deoxygenation, the globin unites are tightly bound in a
tense (T) configuration which reduces the affinity of the molecule for
O2. When O2 is first bound, the bonds holding the globin unites are
released, producing a relaxed (R) configuration which expose more
O2 binding sites. The net result is 500 fold increases in O2 affinity. In
the tissue this reaction is revered releasing O2.
The oxygen-hemoglobin dissociation curve, the curve
relating percentage saturation of the O2-carrying power of the
hemoglobin to the PO2. It has a characteristic sigmoid shape
due to the T-R interconversion.
When blood is equilibrated with 100% O2 (PO2 =760 mm Hg),
the normal hemoglobin become 100% saturated, when fully
saturated, each gram of normal of normal hemoglobin contain
1.39 mL of O2. However, blood normally contains small
amounts of inactive hemoglobin derivatives, and the
measured value in vivo is lower. The traditional figure is 1.34
mL of O2. The hemoglobin concentration in normal blood is 15
g/dL. Therefore, each dL of blood contains 20.1 mL (1.34mL X
15) of O2 bound to hemoglobin when the hemoglobin 100%
saturated. The amount of dissolved O2 is a liner function of
the PO2 (0.003 mL/dL blood / mm Hg PO2).
➢ In vivo the hemoglobin in the blood at the end of the
pulmonary capillaries is about 97.5% saturated with O2
(PO2=97 mm Hg). Because of a slight admixture with the
venous blood that bypasses the pulmonary capillaries
(physiological shunt). The hemoglobin in the systemic arterial
blood is only 97% saturated. The arterial blood therefore
contains a total about 19.8 mL of O2 per dL. 0.29 mL in a
solution and 19.5 mL bound to hemoglobin. In venous blood
at rest, the hemoglobin is 75% saturated and the total O2
content is about 15.2 mL/dL. 0.12mL in a solution and 15.1 mL
bound to hemoglobin. Thus, at rest tissue removes about 4.6
mL of O2 from each dL of blood passing through them. In this
way, 250 mL of O2 per minute is transported from the blood to
the tissue at rest.