    Factors that affect the standard dissociation curve The strength with which oxygen binds to hemoglobin is affected by several factors. These factors shift or reshape the oxyhemoglobin dissociation curve. A rightward shift indicates that the hemoglobin under study has a decreased affinity for oxygen. This makes it more difficult for hemoglobin to bind to oxygen (requiring a higher partial pressure of oxygen to achieve the same oxygen saturation), but it makes it easier for the hemoglobin to release oxygen bound to it. The effect of this rightward shift of the curve increases the partial pressure of oxygen in the tissues when it is most needed, such as during exercise, or hemorrhagic shock. In contrast, the curve is shifted to the left by the opposite of these conditions. This leftward shift indicates that the hemoglobin under study has an increased affinity for oxygen so that hemoglobin binds oxygen more easily, but unloads it more reluctantly. Left shift of the curve is a sign of hemoglobin's increased affinity for oxygen (e.g. at the lungs). Similarly, right shift shows decreased affinity, as would appear with an increase in either body temperature, hydrogen ions, 2,3-bisphosphoglycerate (2,3-BPG) concentration or carbon dioxide concentration. Effects of ITPP Myo-inositol trispyrophosphate (ITPP), also known as OXY111A, is an inositol phosphate that causes a rightward shift in the oxygen hemoglobin dissociation curve through allosteric modulation of hemoglobin within red blood cells. It is an experimental drug intended to reduce tissue hypoxia. The effects appear to last roughly as long as the affected red blood cells remain in circulation.       
Right and left shift of the Curve Right and left shift of the oxygen haemoglobin dissociation curve In the figure when curve Shift Right at 40 mmHg of PO2 the Haemoglobin saturation is around 59\%. And when curve Shifts Left at 40 mmHg of PO2 the Haemoglobin saturation is around 72\%. This shows that on Right shift the affinity of oxygen to bind Haemoglobin decreases and on Left shift the affinity of oxygen to bind Haemoglobin increases. Factors that affect the standard dissociation curve The strength with which oxygen binds to hemoglobin is affected by several factors. These factors shift or reshape the oxyhemoglobin dissociation curve. A rightward shift indicates that the hemoglobin under study has a decreased affinity for oxygen. This makes it more difficult for hemoglobin to bind to oxygen (requiring a higher partial pressure of oxygen to achieve the same oxygen saturation), but it makes it easier for the hemoglobin to release oxygen bound to it. The effect of this rightward shift of the curve increases the partial pressure of oxygen in the tissues when it is most needed, such as during exercise, or hemorrhagic shock. In contrast, the curve is shifted to the left by the opposite of these conditions. This leftward shift indicates that the hemoglobin under study has an increased affinity for oxygen so that hemoglobin binds oxygen more easily, but unloads it more reluctantly. Left shift of the curve is a sign of hemoglobin's increased affinity for oxygen (e.g. at the lungs). Similarly, right shift shows decreased affinity, as would appear with an increase in either body temperature, hydrogen ions, 2,3-bisphosphoglycerate (2,3-BPG) concentration or carbon dioxide concentration. Effects of ITPP Myo-inositol trispyrophosphate (ITPP), also known as OXY111A, is an inositol phosphate that causes a rightward shift in the oxygen hemoglobin dissociation curve through allosteric modulation of hemoglobin within red blood cells. It is an experimental drug intended to reduce tissue hypoxia. The effects appear to last roughly as long as the affected red blood cells remain in circulation. Factor causing Right shift of the curve 1) Increased hydrogen ions (low pH) 2) Increased CO2 This is due to Bohr Effect which says the increase in blood CO2 and hydrogen ions enhances the release of oxygen from the blood in the tissues enhancing oxygenation of blood. 3) Increased temperature (during exercise) The exercising muscle causing increased temperature releases large quantities of CO2, several acids causing release of large H+ ions increases the delivery of oxygen to muscle fibers. This shifts the curve to right. 4) Increased BPG (2, 3-biphosphoglycerate) BPG produced in the response to hypoxia which binds to beta chain of deoxygenated haemoglobin releasing oxygen in the blood and decreasing the affinity of haemoglobin and hence shifts the curve to right. ature Factor causing left shift of the curve 1) Decreased hydrogen ions (high pH) 2) Decreased CO2 3) Decreased temperature
A
Right and left shift of the Curve Right and left shift of the oxygen haemoglobin dissociation curve In the figure when curve Shift Right at 40 mmHg of PO2 the Haemoglobin saturation is around 59\%.
A
And when curve Shifts Left at 40 mmHg of PO2 the Haemoglobin saturation is around 72\%.
A
This shows that on Right shift the affinity of
A
oxygen to bind Haemoglobin decreases and on Left shift the affinity of oxygen to bind Haemoglobin increases.
A
Factor causing Right shift of the curve 1) Increased hydrogen ions (low pH)
A
2) Increased CO2
A
This is due to Bohr Effect which says the increase in blood CO2 and hydrogen ions enhances the release of oxygen from the blood in the tissues enhancing oxygenation of blood. 3) Increased temperature (during exercise) The exercising muscle causing increased temperature releases large quantities of CO2, several acids causing release of large H+ ions increases the delivery of oxygen to muscle fibers. This shifts the curve to right. 4) Increased BPG (2, 3-biphosphoglycerate) BPG produced in the response to hypoxia which binds to beta chain of deoxygenated haemoglobin releasing oxygen in the blood and decreasing the affinity of haemoglobin and hence shifts the curve to right.
A
ature
A
Factor causing left shift of the curve 1) Decreased hydrogen ions (high pH)
A
2) Decreased CO2
A
3) Decreased temperature