The oxygen affinity of 3-oxy-haemoglobin is 300 times greater than that of deoxy-haemoglobin.

Hb Bassett is a hemoglobin variant that exhibits a very reduced oxygen affinity (Abdulmalik et al., 2004).

In the presence of disease or other conditions that change the haemoglobin's oxygen affinity and, consequently, shift the curve to the right or left, the P50 changes accordingly.

For example, embryonic and fetal hemoglobin have higher oxygen affinity than adult hemoglobin giving them improved functionality in hypoxic environments such as the uterus.

The oxygen affinity of 3-oxy-hemoglobin is 300 times greater than that of deoxy-hemoglobin.

Myoglobin, by nature, has a higher oxygen affinity than hemoglobin.

These bind to a phosphate "pocket" on the fish hemoglobin molecule, which stabilizes the tense state and therefore decreases oxygen affinity.

Its mega-hemocyanin have unusually high oxygen affinities.

This requires the fetal hemoglobin to have a higher oxygen affinity than that of the maternal carrier.

This implies important functional consequences for oxygen affinity.