Structure of Hemoglobin

Structure of Hemoglobin


HAEMOGLOBIN

  • Haemoglobin a tetrameric protein of erythrocytes.
  • A single heme consist of single iron in ferrous state (Fe+2).

Structure of Hemoglobin-

  • Secondary structure
  • Tertiary structure
  • Quaternary structure

Genetics of alpha and Beta chains-

  • α-like globin genes on chromosome 16.
  • β-like globin genes on chromosome 11.

Types of Hemoglobin-

  • Embryonic haemoglobins
  1. Hb Portland ?2γ2
  2. Hb Gower I- ?2ε2
  3. Hb Gower II- α2ε2
  • Fetal Hemoglobins
  1. Hb F- α2γ2
  • Adult Hemoglobins
  1. Hb A1 – α2β2
  2. Hb A2 – α2δ2

Charateristics of Hemoglobin

  • Slower electrophoretic mobility
  • Increased resistance to Alkali Denaturation
  • Decreased Interaction with 2, 3 BPG.

Interactions of Hemoglobin with 2, 3 BPG

  • 2, 3 BPG is an intermediate of Glycolysis.
  • Synthesized of 2, 3 BPG shunt or Rapaport Leubering Cycle.
  • Binding of 2, 3 BPG in the curve shifts ODC to right.
GLOBIN-
  • Each polypeptide chain is made up of helical segments.
  • Heme binding to hydrophobic pocket.

Exam Important

  • A single heme consist of single iron in ferrous state (Fe+2).

Genetics of alpha and Beta chains-

  • α-like globin genes on chromosome 16.
  • β-like globin genes on chromosome 11.

Types of Hemoglobin-

  • Embryonic haemoglobins
  1. Hb Portland ?2γ2
  2. Hb Gower I- ?2ε2
  3. Hb Gower II- α2ε2
  • Fetal Hemoglobins
  1. Hb F- α2γ2
  • Adult Hemoglobins
  1. Hb A1 – α2β2
  2. Hb A2 – α2δ2

Charateristics of Hemoglobin

  • Slower electrophoretic mobility
  • Increased resistance to Alkali Denaturation
  • Decreased Interaction with 2, 3 BPG.
  • Binding of 2, 3 BPG in the curve shifts ODC to right.
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