HEMOGLOBIN

Dr. Subathra T A

SCHEMA

Introduction
Normal hemoglobin content
Functions
Structure
Types of normal hemoglobin
Abnormal hemoglobin
Abnormal hemoglobin derivatives
Synthesis
Destruction
Iron metabolism

INTRODUCTION
Hemoglobin (Hb) is the iron containing coloring matter of red
blood cell (RBC)
Chromoprotein forming 95% of dry weight of RBC and 30%
to 34% of wet weight
Function - carry the respiratory gases,oxygen and carbon
dioxide and buffer
Molecular weight - 68,000

NORMAL HEMOGLOBIN CONTENT

Average hemoglobin (Hb) content - 14 to 16 g/dL.
Age
At birth : 25 g/dL
After 3rd month : 20 g/dL
After 1 year : 17 g/dL
From puberty onwards : 14 to 16 g/dL
Sex
In adult males : 15 g/dL
In adult females : 14.5 g/dL

FUNCTIONS
TRANSPORT OF RESPIRATORY GASES
1. Oxygen from the lungs to tissues.
2. Carbon dioxide from tissues to lungs.
Transport of Oxygen
oxygen + hemoglobin = oxyhemoglobin. (Unstable)
Iron - ferrous state.
Reduced hemoglobin or ferrohemoglobin.
Transport of Carbon Dioxide
CO2 + hemoglobin = carbhemoglobin (unstable)
BUFFER ACTION

STRUCTURE
Conjugated protein (globin) + Iron containing pigment heme.
Myoglobin (oxygenbinding pigment in muscles)
Neuroglobin (oxygenbinding pigment in brain).
IRON
Normally - ferrous (Fe2+) form (unstable)
Ferric (Fe3+) form (stable)

PORPHYRIN
The pigment part of heme is called porphyrin.
Four pyrrole rings (tetrapyrrole) called, I, II, III and IV.
The pyrrole rings are attached to one another by methane
(CH4) bridges.
The iron is attached to N of each pyrrole ring and N of globin
molecule.
GLOBIN
Globin contains four polypeptide chains. Among the four
polypeptide chains, two are chains and two are -chains

TYPES OF NORMAL HEMOGLOBIN

Hemoglobin is of two types:

1. Adult hemoglobin HbA
2. Fetal hemoglobin HbF
Replacement of fetal hemoglobin by adult hemoglobin starts
immediately after birth. It is completed at about 10th to 12th week
after birth.
Both the types of hemoglobin differ from each other structurally
and functionally.

Structural Difference
Adult hemoglobin, two -chains and two -chains
In fetal hemoglobin, two chains and two -chains
Functional Difference
Fetal hemoglobin has more affinity for oxygen than that of adult
hemoglobin.
Oxygenhemoglobin dissociation curve of fetal blood is shifted to
left

ABNORMAL HEMOGLOBIN
Hemoglobinopathies
Hemoglobin in thalassemia and related disorders
Hemoglobinopathies
- genetic disorder caused by abnormal polypeptide chains of
hemoglobin.
- Hemoglobin S ,C,E & M
Hemoglobin in Thalassemia and Related Disorders
- -thalassemia, the -chains are decreased, absent or abnormal
- -thalassemia, the -chains are decreased, absent or abnormal

 ABNORMAL HEMOGLOBIN DERIVATIVES

Abnormal hemoglobin derivatives are:
1. Carboxyhemoglobin
2. Methemoglobin
3. Sulfhemoglobin.
Normal percentage of hemoglobin derivatives in total
hemoglobin:
Carboxyhemoglobin : 3% to 5 %
Methemoglobin : less than 3%
Sulfhemoglobin : trace (undetectable).

CARBOXYHEMOGLOBIN
carbon monoxide + hemoglobin.
Hemoglobin has 200 times more affinity for carbon monoxide
than oxygen, it hinders the transport of oxygen
Signs and Symptoms of Carbon Monoxide Poisoning
- < 1% of CO, the Hb saturation is 15% to 20% and mild symptoms
like headache and nausea appear
- > 1% CO, the Hb saturation is 30% to 40%
i. Convulsions
ii. Cardiorespiratory arrest
iii. Unconsciousness and coma.
- Hb saturation increases above 50%, death occurs

METHEMOGLOBIN
Iron molecule of hemoglobin is oxidized from normal ferrous
state to ferric state.
Also called ferrihemoglobin.
Nicotinamide adenine dinucleotide (NADH) system, which
operates through two enzymes:
1. Diaphorase I (nicotinamide adenine dinucleotide phosphate
[NADPH]dependent reductase): 95% of the action.
2. Diaphorase II (NADPHdependent methemoglobin
reductase): 5% of the action.
These two enzymes prevent the oxidation of ferrous iron into
ferric iron.

DESTRUCTION OF HEMOGLOBIN
- Lifespan of RBC - 120 days,
-destroyed in the reticuloendothelial system, spleen
-hemoglobin is degraded in the reticuloendothelial cells and split into
globin and heme.
Globin is utilized for the resynthesis of hemoglobin.
Heme is degraded into iron and porphyrin.
Iron is stored in the body as ferritin and hemosiderin, which are reutilized
for the synthesis of new hemoglobin.
Porphyrin is converted into a green pigment called biliverdin.
Inhuman being, most of the biliverdin is converted into a yellow
pigment called bilirubin.
Bilirubin and biliverdin are together called the bile pigments

THANK YOU