What does the oxyhemoglobin dissociation curve tell us?

The oxyhemoglobin dissociation curve (OHDC) indicates the relationship between the oxygen saturation of hemoglobin (Sao2) and the partial pressure of arterial oxygen (Pao2). It indirectly indicates arterial hemoglobin saturation, measured as oxygen saturation by pulse oximetry (Spo2).

How does anemia affect p50?

p50 is the oxygen tension when hemoglobin is 50 % saturated with oxygen. When hemoglobin-oxygen affinity increases, the oxyhemoglobin dissociation curve shifts to the left and decreases p50. When hemoglobin-oxygen affinity decreases, the oxyhemoglobin dissociation curve shifts to the right and increases p50 (Figure 1).

What shifts the oxyhemoglobin dissociation curve to the left?

Carbon Monoxide The binding of one CO molecule to hemoglobin increases the affinity of the other binding spots for oxygen, leading to a left shift in the dissociation curve. This shift prevents oxygen unloading in peripheral tissue and therefore the oxygen concentration of the tissue is much lower than normal.

What causes a shift to the right in the oxyhemoglobin dissociation curve?

Factors which result in shifting of the oxygen-dissociation curve to the right include increased concentration of pCO2, acidosis, raised temperature and high concentrations of 2,3 diphosphoglycerate (2,3 DPG). These factors, in effect, cause the Hb to give up oxygen more readily.

What does P50 value indicate?

The P50 is the oxygen tension at which hemoglobin is 50% saturated. The normal P50 is 26.7 mm Hg. A rightward shift increases P50 and lowers hemoglobin’s affinity for oxygen, thus displacing oxygen from hemoglobin and releasing it to the tissues.

How do you interpret oxygen dissociation curve?

The oxygen dissociation curve can be shifted right or left by a variety of factors. A right shift indicates decreased oxygen affinity of haemoglobin allowing more oxygen to be available to the tissues. A left shift indicates increased oxygen affinity of haemoglobin allowing less oxygen to be available to the tissues.

What 4 factors affect hemoglobin’s affinity for oxygen?

The affinity of hemoglobin is affected by temperature, hydrogen ions, carbon dioxide, and intraerythrocytic 2,3-DPG, with all these factors mutually influencing each other.

What factors increase oxyhemoglobin dissociation?

The oxygen–hemoglobin dissociation curve can be displaced such that the affinity for oxygen is altered. Factors that shift the curve include changes in carbon dioxide concentration, blood temperature, blood pH, and the concentration of 2,3-diphosphoglycerate (2,3-DPG).

Are P50 and KD the same?

For oxygen binding proteins the KD is also referred to as the “p50”, the amount of oxygen required to give a fractional saturation of Y=0.5. In the case of myoglobin, the KD is 2-3 torr. The affinity increases as more oxygen is bound, favoring loading of O2 in the lungs.

What causes oxygen dissociation curve?

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.

When to worry about oxygen saturation?

Oxygen saturation levels less than 90 percent should be considered a medical emergency, WHO advises. Symptoms of hypoxemia , including cyanosis, or a bluish coloring to the skin and mucus membranes, aren’t evident until oxygen saturation falls below 90 percent.

Why is that oxygen dissociation curve sigmoid?

The oxygen dissociation curve has a sigmoid shape because of the co-operative binding of oxygen to the 4 polypeptide chains . Co-operative binding means that haemoglobin has a greater ability to bind oxygen after a subunit has already bound oxygen.

What is the saturation point of oxygen?

When blood passes through the lungs, 95 to 100 per cent of the body’s red blood cells bind to or become saturated with oxygen. Normal oxygen saturation levels are between 95 and 100 per cent.