in the partial
pressure of oxygen, hence a reduced
hemoglobin. Thus, the oxygen transport system is ideally designed to
perform the tasks
on-demand metabolic adjustments. This is even
illustrated when oxygen
from hemoglobin to
myoglobin during greater muscle tissue demand.
myoglobin for oxygen
significantly greater than that
Oxygen saturation curve displaying
S-shaped characteristics. Normal
arterial and venous blood 02 saturations are
The oxygen affinity decreases with decreasing pH. This is termed the
Bohr effect by which changes in blood
which affects blood pH,
indirectly also influence hemoglobin-oxygen affinity.
Hemoglobin consists of four polypeptide chains or globins and four
disc-shaped molecular ring
groups, allowing binding of four
Once bound with oxygen, the iron atoms in
hemoglobin gives it the red color.
Optical absorptions of hemoglobin
and oxy-hemoglobin (Fig.
can be readily monitored by near-
infrared spectroscopy. The isobestic point, when the
equal which can be used as a reference, is at