Assertion: hemoglobin's oxygen | /r/HasProperty | released
Facets:
value: by heating the material
type: MANNER
Source sentences:
text: While it is important for oxygen to be carried to different areas of the body, it is even more important for the oxygen to be released when needed.
text: It is important to leave the myoglobin in the dioxygen form rather than superoxide form when the oxygen is released because the superoxide can be generated by itself to have a new form that gives negative effect on many biological materials, and also the superoxide prevents the iron ion from binding to the oxygen in its ferric state (Metmyoglobin).
text: Thus, as hemoglobin approaches a region of low pH, more oxygen is released.
text: When salt bridges form by the interaction of these interfacial histidine residues and nearby negatively charged amino-acid residues, the deoxygenated hemoglobin structure is favored, and oxygen is released (left image in Figure 8).
text: However, once the oxygen is released, sickle hemoglobin tends to polymerize (line-up) into rigid rods that alter the shape of the red blood cell.
text: The stored oxygen can be released again when and where it is needed.
text: Crystals are black when they are saturated with oxygen and pink when the oxygen has been released again.
text: The oxygen can be released by gently heating the material or subjecting it to low oxygen pressures.
text: However, once the oxygen is released, sickle hemoglobin tends to polymerize (line-up) into rigid rods that alter the shape of the red blood cell.