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Dr. Niranjan Murthy H.L Assistant Professor Dept of Physiology SSMC

This document provides an overview of hemoglobin including its structure, types, synthesis, fate, derivatives, clinical applications like anemias and hemoglobinopathies. Hemoglobin is composed of an iron-protoporphyrin complex bound to globin proteins. It carries oxygen from the lungs to tissues and carbon dioxide back. Deficiencies can cause anemia. Common types include adult HbA, fetal HbF, and HbS in sickle cell anemia. Hemoglobin is broken down in the spleen after RBCs are destroyed.

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2K views22 pages

Dr. Niranjan Murthy H.L Assistant Professor Dept of Physiology SSMC

This document provides an overview of hemoglobin including its structure, types, synthesis, fate, derivatives, clinical applications like anemias and hemoglobinopathies. Hemoglobin is composed of an iron-protoporphyrin complex bound to globin proteins. It carries oxygen from the lungs to tissues and carbon dioxide back. Deficiencies can cause anemia. Common types include adult HbA, fetal HbF, and HbS in sickle cell anemia. Hemoglobin is broken down in the spleen after RBCs are destroyed.

Uploaded by

nirilib
Copyright
© Attribution Non-Commercial (BY-NC)
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPT, PDF, TXT or read online on Scribd
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Dr. Niranjan Murthy H.

L
Assistant Professor
Dept of Physiology
SSMC
HAEMOGLOBIN
• INTRODUCTION
• STRUCTURE
• TYPES
• SYNTHESIS
• FATE
• DERIVATIVES
• CLINICAL- ANAEMIAS
- HAEMOGLOBINOPATHIES
- PORPHYRIAS
• Pigment present inside RBCs

• Carries O2 and CO2

• Responsible for red color of blood

• Deficiency is called anaemia


STRUCTURE OF HEMOGLOBIN
• Iron-protoporhyrin-globin forms a subunit

• 4 subunits join to form a molecule of Hb

• Iron is in ferrous ( Fe2+) form

• Fe2+ binds 4 pyrrole rings, polypeptide


chain and a molecule of O2
• 4 pyrroles join to form a ring called
porphyrins
• 4 polypeptide chains constitute
globin
• α,β,γ and δ are four important
polypeptide chains
• α chain has 141 a.a
• β and γ chain have 146 a.a
TYPES OF HEMOGLOBIN
• HbA- Adult Type- α2β2
• HbA2- 2% of adult Hb- α2δ2
• HbF- Fetal Type- α2γ2
• Hb gower1- ε2ζ2
• Hb gower2- ζ2β2
SYNTHESIS
SUCCINYL Co-A + GLYCINE
ALA synthase
δ-AMINOLEVUNIC ACID

PORPHOBILINOGEN

PROTOPORPHYRIN IX
Fe2+ haem synthase

HAEM
GLOBIN

HAEMOGLOBIN
FATE OF HAEMOGLOBIN
• RBCs are destroyed in RES ( mainly spleen
and bone marrow) after 120 days of life.

• Macrophages phagocytose – hemolyse -


degrade haemoglobin – form Bilirubin –
transport to liver with albumin – conjugated
and detoxified – secreted in bile.
H a e m o g lo b in

H aem G lo b in

P r o t o p o r p h y r in Iro n CO A m in o a c id p o o l

B iliv e r d in ir o n p o o l

B ilir u b in
DERIVATIVES OF Hb
1) Oxyhaemoglobin (HbO2) – oxygenation reaction
– combination with Fe 2+

2) Carbaminohaemoglobin ( CO2Hb)  carbon


dioxide combines with globin part

3) Carboxyhaemoglobin (COHb)  carbon


monoxide binds with Fe 2+
{ 250 times more affinity than oxygen}
4) Methhaemoglobin ( HHb) 
oxidized haemoglobin

5) Sulfhaemoglobin

6) Glycated haemoglobin (HbA1c) 


Glucose attached to terminal Valine
in β chain. – integrated index of
Diabetic control over 4 to 6 weeks
FUNCTIONS OF HEMOGLOBIN
• 1. Transports O2 from lungs to tissues in the
form of oxy-hemoglobin
• 2. Transports CO2 from tissues to lungs in the
form of carbamino-hemoglobin:- 30% of total
CO2 transport
• 3. Acts as a buffer- important in acid-base
balance- 6 times more than plasma proteins
APPLIED ASPECTS
• Normal Hb value :
Males  14 – 18 gm/dL
Females  12 – 16 gm/dL

# ANAEMIAS
# HAEMOGLOBINOPATHIES
# PORPHYRIAS
ANAEMIAS
Classification:

I . Based on severity.

v) Mild – 8-12gm/dL
vi) Moderate – 5-8gm/dL
vii) Severe - < 5gm/dL
II) Based on morphology of RBCs

• Normocytic normochromic – eg. Acute


blood loss
• Macrocytic – eg Vit B12 & Folic acid
deficiency
• Microcytic hypochromic – iron
deficiency anaemia
III) Based on aetiology :
• Blood loss – RTA, Surgeries
• Haemolytic anaemias – congenital,
malaria
• Bone marrow depression- Aplastic
anaemia
• Nutritional anaemias- iron deficiency,
megaloblastic,
• Genetic causes- thalassaemia
HAEMOGLOBINOPATHIES
Sickle cell anaemia:
Valine replaces glutamate in the 6th position of β chain.
Is common in African blacks
Confers resistance against malaria
Hb crystallizes & takes sickle shape under hypoxic
conditions.
Increased RBC sequestration
THALASSAEMIA
• Reduced or absent synthesis of globin
chains.
Types:- alpha & Beta
- Major & Minor
β-thalassemia major cooley’s anaemia
Treatment  # Transfusion – packed red
cell is preferred.
# Splenectomy
# Bone Marrow Transplant
PORPHYRIAS
• DEF: Inherited disorders involving specific
enzymes in heme biosynthetic pathway
• TYPES:
• a) Hepatic porphyrias
i) ALA dehydratase deficient porphyrias
ii) Acute intermittent porphyrias
iii) Porphyria cutanea tarda
b) Erythropoetic porphyrias
i) X-linked sideroblastic anemias
ii) Congenital erythropoetic porphyrias
Other molecules containing Haem:-
i) Myoglobin – present in muscles
- combination with single
polypeptide chain.
ii) Neuroglobin – present in CNS
iii) Cytochrome enzymes – present in
mitochondria
iv) Peroxidases

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