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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