Hemoglobin alpha-chain fragments (123-136)

1450.7 g/mol

1449.80789561 g/mol

586 Ų

This means that the oxygen binding curve for fetal hemoglobin is left-shifted (i.e., a higher percentage of hemoglobin has oxygen bound to it at lower oxygen tension), in comparison to that of adult hemoglobin

Investigated for use/treatment in blood (blood forming organ disorders, unspecified) and hemorrhage.

There is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis

A heme group is made up of iron (Fe) ion (charged atom) located in a heterocyclic ring, which is also called a porphyrin ring. The site of oxygen binding, the iron ion, binds with the nitrogens located in the center of the porphyrin ring. The iron ion binds with high affinity to the globular protein through the imidazole ring of the F8 residue on histidine which is found below the porphyrin ring. A sixth position can bind reversibly to oxygen, completing the formation of the octahedral group. One oxygen atom binds Fe and the other is found to protrude at an angle. When oxygen is not bound to Fe, a water molecule (weakly bound) fills the site, producing a distorted shape, often described as an octahedron.

Hb (123-136)