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Factors Affecting The Affinity of Hemoglobin For Oxygen

Three factors affect the affinity of hemoglobin for oxygen: temperature, pH, and 2,3-BPG. Higher temperatures and lower pH levels decrease affinity, shifting the oxygen-hemoglobin dissociation curve to the right. Increased levels of 2,3-BPG also decrease affinity by binding to deoxyhemoglobin. The concentration of 2,3-BPG is affected by pH, exercise, altitude, thyroid hormones, and other factors.

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47 views9 pages

Factors Affecting The Affinity of Hemoglobin For Oxygen

Three factors affect the affinity of hemoglobin for oxygen: temperature, pH, and 2,3-BPG. Higher temperatures and lower pH levels decrease affinity, shifting the oxygen-hemoglobin dissociation curve to the right. Increased levels of 2,3-BPG also decrease affinity by binding to deoxyhemoglobin. The concentration of 2,3-BPG is affected by pH, exercise, altitude, thyroid hormones, and other factors.

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Factors affecting the affinity of Hemoglobin

For oxygen
Three important conditions affecting the oxygen-hemoglobin
dissociation curve:
• Temperature: arise in temperature shift the curve to the right. When
the curve shift in this direction, a higher PO2 is required for
hemoglobin to bind a given amount of O2. Conversely, a fall in
temperature shifts the curve to the left, and a lower PO2 is required
to bind a given amount of O2. A convenient index of such a shifts is
the P50, the PO2 at which the hemoglobin is half saturated with O2.
the higher the P50, the lower the affinity of hemoglobin for O2.

• PH: a fall in Ph shifts the curve to the right, and the rise in PH shifts
the curve to the left. The decrease in O2 affinity of hemoglobin when
the PH of the blood falls is called the Boher effect and is closely
related to the fact that deoxygenated hemoglobin bind H more
actively than dose oxyhemoglobin. The PH of the blood falls as its
CO2 contents increases, so that when the PCO2 rises, the curve shift
to the right and the P50 rises.
• 2,3-BPG: is very plentiful in the red cells, it is formed from 3-
phosphoglyceraldehyde. It is a highly charged anion that bind
to the B chains of the deoxyhemoglobin. One molecule of
deoxyhemoglobin bind one molecule 2,3-BPG. In effects:
HbO2 + 2,3-BPG = Hb – 2,3-BPG + O2
In this equilibrium, an increase in the concentration of 2,3-
BPG shifts the reaction to the right. Causing more O2 to
liberate.
Factors affecting the concentration of 2,3-BPG in the
red cells include:
❖ PH: the 2,3-BPG concentration falls when the PH is low.
❖ Thyroid hormones, growth hormone, and androgens increase
the concentration of 2,3-BPG and the P50.
❖ Exercise has been reported to produce an increase in 2,3-BPG
within 60 minutes, although the rise may not occur in trained
athletes. The P50 is also increased during exercise, because the
temperature rises in active tissues and the CO2 and the
metabolites accumulate, lowering the PH.
❖ Ascend to high altitude trigger a substantial rise in 2,3-BPG
concentration in red cells, with a consequent increases in P50
and increase in the availability of O2 to the tissue.
❖ The affinity of fetal hemoglobin (hemoglobin F) for O2 which is
greater than that for adult hemoglobin (hemoglobin A),
facilitates the movement of O2 from the mother to the fetus.
The cause of this greater affinity is the poor binding of 2,3-
BPG by the Y chains that replace B chains in fetal hemoglobin.

❖ Red blood cells 2,3-BPG concentration is increased in anemia


and in varity of diseases in which there is chronic hypoxia. This
facilitates the delivery of O2 to the tissues by raising the PO2 at
which O2 is released in the peripheral capillaries.

❖ In bank blood that stored, the 2,3-BPG level falls and the
ability of this blood to release O2 to the tissue is reduced.
Myoglobin

Myoglobin is an iron-containing pigment found in skeletal


muscles. It resembles hemoglobin but bind 1 rather than 4
mol of O2 per mole. Its dissociation curve is rectangular rather
than sigmoid curve. Because its curve is to the left of the
hemoglobin curve, its take up O2 from hemoglobin in the
blood. It releases O2 only at low PO2 values, put the PO2 in
exercising muscle is close to zero. The myoglobin content is
greatest in muscles specialized for sustained contractions. The
muscles blood supply is compressed during such contractions,
and myoglobin may provide O2 when blood flow is cut off.
CARBON DIOXIDE TRANSPORT

Fate of carbon Dioxide in Blood


The solubility of CO2 in blood is about 20 times that of O2,
therefore, considerably more CO2 than O2 is present in simple
solution at equal partial pressure. The CO2 that diffuses into
red blood cells is rapidly hydrated to H2CO3 .
because of the presence of carbonic anhydrase. The H2CO3
dissociates to H+ and HCO3- and the H+ is buffered, primarily
by hemoglobin, while the HCO3- enters the plasma.
Some of the CO2 in the red cells reacts with amino groups of
the hemoglobin and other proteins ( R ), forming carbamino
compounds.
Since deoxygenated hemoglobin binds more H+ than
oxyhemoglobin does and forms carbamino compounds more
readily, binding of O2 to hemoglobin reduces its affinity for CO2
(Haldane effect). Consequently venous blood carry more CO2
than arterial blood, CO2 uptake is facilitated in the tissue, and
CO2 release is facilitated in the lung. About 11 % of the CO2
added to the blood in the systemic capillaries is carried to the
lungs as carbamino-CO2.
In the plasma, CO2 reacts with the plasma proteins to form
small amounts of carbamino compounds, and small amount
of CO2 are hydrated but the hydration reaction is slow in the
absence of carbonic anhydrase.
Chloride Shift
Since the rise in HCO3- content of red cells is much greater than
that in the plasmas blood passes in the capillaries, about 70% of the
HCO3- formed in the red cells enters the plasma. The excess HCO3-
leaves the red cells in exchange for Cl-. This process is mediated by
Band 3, a major membrane protein. This exchange is called the
chloride shift. Because of it, the Cl- content of the red cell in venous
blood is therefore significantly greater than in arterial blood.
Note that for each CO2 molecule added to a red cell, there is an
increase of one osmotically active particle in the cell-either an
HCO3- or Cl- in the red cell, consequently, the red cells take up
water and increase in size. For this reason, plus the fact that a small
amount of fluid in the arterial blood return via the lymphatics
rather than veins, the hematocrit of venous blood is normally 3%
greater than that of the arterial blood. In the lungs, the Cl- moves
out of the cells and they shrinks.
Summary of Carbon Dioxide Transport
In plasma 1. dissolved
2. formation of carbamino compounds with plasma
proteins
3. hydration, H+ buffered, HCO3 in plasma

In red blood cells


➢ dissolved
➢ formation of carbamino-Hb
➢ Hydration, H+ buffered, 70% of HCO3 enters the plasma
➢ Cl- shifts into cells, mosm in cells increases.

➢ In the tissue, CO2 is added to the blood, the PH of the blood drops
from 7.40 to 7.36. in the lungs the process are reversed, and the
CO2 is discharged into the alveoli, in this fashion, 200 mL of CO2 per
minute at rest and much larger amounts during exercise are
transported from the tissue to the lungs and excreted.

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