Hemoglobin Adaptations

Hemoglobin

An iron-containing respiratory pigment found within red blood cells

Partial pressure

Pressure exerted by each of the gases in a mixture of gases

pO2

Partial Pressure of o2

High pO2

Hemoglobin has high affinity for oxygen, therefore binding to O2 in the lungs and release it in the tissues

Low pO2

hemoglobin will have low affinity for oxygen and release O2 in the cells

The bohr shift

describes how hemoglobin's affinity for oxygen decreases in acidic environments or in the presence of high carbon dioxide levels.

How does bohr shift occur?

Due to carbon dioxide binding to an allosteric site on the hemoglobin and thus changing its shape - new shape causes release of oxygen

Myoglobin

oxygen transport protein in muscles

Function of myoglobin

to release oxygen when pO2 in the muscles are very low → leading to delay the onset of anaerobic respiration during vigorous exercise

Moderate pO2 (Myoglobin)

Adult hemoglobin release O2 and myoglobin binds it

Myoglobin vs Haemoglobin Graph

Fetal hemoglobin

Hemoglobin of a fetus

Fetal hemoglobin vs adult