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FORMATION OF HAEMOGLOBIN
Haemoglobin, is the iron-containing oxygen-transport metalloprotein in the red blood
cells (erythrocytes) of almost all vertebrates as well as the tissues of some invertebrates.
Haemoglobin in blood carries oxygen from the lungs to the rest of the body.
Haemoglobin develops in cells in the bone marrow that become red blood cells. When
red cells die, haemoglobin is broken up: iron is removed and transported to the bone
marrow by proteins called transferrins, and used again in the production of new red blood
cells.
• Haemoglobin is a protein made up of four polypeptide chains (α1, α2, β1, and β2).
• Each chain is attached to a heme group composed of porphyrin (an organic ring
like compound) attached to an iron atom.
• These iron-porphyrin complexes coordinate oxygen molecules reversibly, an ability
directly related to the role of haemoglobin in oxygen transport in the blood.
 Haemoglobin (Hb) is synthesized in a complex series of steps.
• The heme part is synthesized in a series of steps in the mitochondria and
the cytosol of immature red blood cells, while the globin protein parts are
synthesized by ribosomes in the cytosol.
• Production of Hb continues in the cell throughout its early development from
the proerythroblast to the reticulocyte in the bone marrow.
• Haemoglobin synthesis is a complicated process. This takes place in the red blood cells.
– Amino acids are assembled in the ribosomes and give rise to α2 β2 globulin.
– Heme molecule will have protoporphyrin by the chemical combination of glycine and
succinyl CoA in the presence of Vitamin B6 and form heme.
– Transferrin gives Iron which will combine with the heme molecule.
• Heme molecule consists of protoporphyrin protein and iron (Fe++).
• Globulin consists of four polypeptide chains (α1, α2, β1, and β2).

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Formation of heamoglobin / B.pharmacy 2 semester

  • 1. FORMATION OF HAEMOGLOBIN Haemoglobin, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates as well as the tissues of some invertebrates. Haemoglobin in blood carries oxygen from the lungs to the rest of the body. Haemoglobin develops in cells in the bone marrow that become red blood cells. When red cells die, haemoglobin is broken up: iron is removed and transported to the bone marrow by proteins called transferrins, and used again in the production of new red blood cells.
  • 2. • Haemoglobin is a protein made up of four polypeptide chains (α1, α2, β1, and β2). • Each chain is attached to a heme group composed of porphyrin (an organic ring like compound) attached to an iron atom. • These iron-porphyrin complexes coordinate oxygen molecules reversibly, an ability directly related to the role of haemoglobin in oxygen transport in the blood.  Haemoglobin (Hb) is synthesized in a complex series of steps. • The heme part is synthesized in a series of steps in the mitochondria and the cytosol of immature red blood cells, while the globin protein parts are synthesized by ribosomes in the cytosol. • Production of Hb continues in the cell throughout its early development from the proerythroblast to the reticulocyte in the bone marrow.
  • 3. • Haemoglobin synthesis is a complicated process. This takes place in the red blood cells. – Amino acids are assembled in the ribosomes and give rise to α2 β2 globulin. – Heme molecule will have protoporphyrin by the chemical combination of glycine and succinyl CoA in the presence of Vitamin B6 and form heme. – Transferrin gives Iron which will combine with the heme molecule. • Heme molecule consists of protoporphyrin protein and iron (Fe++). • Globulin consists of four polypeptide chains (α1, α2, β1, and β2).