Hemoglobin is the red pigment found in red blood cells that is responsible for transporting oxygen and carbon dioxide throughout the body. It is made up of heme and globin proteins. Hemoglobin has a molecular weight of 68,000 and is a globular protein. It is synthesized in immature red blood cells. Normal hemoglobin levels vary between individuals based on factors like age, sex, and physiological state. The structure of hemoglobin involves heme, which contains an iron atom, and globin, which is made up of protein chains that attach to heme. Hemoglobin transports oxygen by binding oxygen molecules to the iron in its heme groups.

2. Hemoglobin = Heme + globin ( protein )
Red pigment
 Present in RBC of Blood.
 Made up of Iron, Heme protein conjugated protein & Chromo protein.
Molecular weight is 68000.
 Globular proteins.
Immature RBCs synthesis Hb.
HEMOGLOBIN

3. NORMAL VALUES OF HEMOGLOBIN
• Fetus – 16-18 gm/dl
• Newborn – 20-24 gm/dl.
• Transfusion from placenta
• Haemoconcentration
• Males - 14 – 17 gm/100ml
• Females- 12 – 15 gm/100ml

4. STRUCTURE OF HAEMOGLOBIN.
• Heme = Protoporphyrin + Iron
• Protoporphyrin = Iron free Heme
• Protoporphyrin consist of 4 pyrrol rings.
• Iron have 6 coordination, 4 bind with these 4 pyrrol rings of Protoporphyrin, 1
bind with histidine ( amino acid ) from globulin and 1 is free (bind to Oxygen , CO2
respectively) Mitochondria is very important for Hemesynthesis
Globin
• Made up of 4 polypeptide chains.
• Globin is HbA
• 2 alpha chains ( ) – 141 amino acids
• 2 Beta chains ( ) – 146 amino acids.

5. ATTACHMENT OF HAEME TO GLOBIN
• 4 units of Haeme attached
to 1 unit of Globin.
• 1 Haemoglobin molecules
contains 4 Iron Atoms
which carry 4 molecules of
oxygen.

6. HAEME IRON-PROTOPORPHYRIN IX
• IRON
• Ferrous form (Fe2+).
• Iron attached to nitrogen atom of each pyrrole ring.
• On iron loose bond for Oxygen
• Carbon monoxide.
• Porphyrin nucleus.
• 4 Pyrrole Rings (Tetrapyrrole)
• Bridges – Methine (CH)
• Side chains – 8
• Methyl (CH3) - 4
• Vinyl (CH.CH2) - 2
• Propionic acid - 2
• (CH2.CH2.COOH)

7. SYNTHESIS OF HEMOGLOBIN

8.  Succinyl-CoA Glycine
(Pyridoxal phosphate)
 Amino -β-ketoadipic acid
(ALA synthetase)
 α amino-δ-Laevulinic acid
(ALA dehydrogenase)
 Porphobilinogen
 Protoporphyrin IX ferrou
Haem globin
Haemoglobin

9. FACTORS
• Role Of Proteins – First class proteins provide amino acids.
• Most imp – food of animal origin, liver, spleen, kidney &
heart
• Intermediate value – muscles
• Least – cereals, dairy products, veg & fruits.

10. FUNCTIONS OF HAEMOGLOBIN
• Transport oxygen to tissues
• Transport Co2 to lungs
• Maintains acid base balance ( As a Buffer

11. VARIETIES OF HAEMOGLOBIN
 Pathological
(Haemoglobinopathies)
• Sickle Cell Haemoglobin.
• Hb C
• Thalassemia
 Physiological
Adult
• Haemoglobin A --4 polypeptide chains
• 2 α (alpha) & 2 β (Beta)
• Haemoglobin A2 -- 2 α (alpha) & 2 δ (Delta)
 Fetal.

12. DERIVATIVES OF HB
• Hb O2 HbO2 Oxyhaemoglobin
• Hb Cyanide Methaemoglobin
• Hb CO2 Carbamino hemoglobin
• Hb CO Carboxy hemoglobin
• Hb H2S Sulphemoglobin.
• Hb Glucose Glycosylated