in an acid environment, oxygen dissociates more readily from hemoglobin; hydrogen ions binding to hemoglobin alter its structure and reduce its oxygen-carrying capacity
The increased oxygen release by hemoglobin in the presence of elevated carbon dioxide levels.
When blood pH decreases, the ability of hemoglobin to bind to oxygen decreases. An adaptation to release oxygen in the oxygen starved tissues in capillaries where respiratory carbon dioxide lowers blood pH
the effect of protons on the binding of oxygen to hemoglobin; promotes both the release of oxygen from hemoglobin in the tissues and the release of carbon dioxide from the blood in the lungs.
Describes the influence of carbon dioxide on the affinity of oxygen binding affinity of hemoglobin. An increasing in the carbon dioxide level decreases the oxygen binding affinity of hemoglobin.
The Bohr effect is a property of hemoglobin first described by the Danish physiologist Christian Bohr in 1904. Because of the Bohr effect, an increase in blood carbon dioxide level, a decrease in p H or increased temperature causes hemoglobin to bind to oxygen with less affinity.
