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HEMOGLOBIN METABOLISM
• Hemoglobin (Hb) is the iron containing coloring material of red blood cell (RBC). It is a
chromoprotein consisting of 95% of dry weight of RBC and 30% to 34% of wet weight.
• Major activity of hemoglobin is to carry the respiratory gases, oxygen and carbon dioxide. It also
behaves as a buffer. Molecular weight of hemoglobin is 68,000.
• NORMAL HEMOGLOBIN CONTENT
• Average hemoglobin (Hb) content in blood is 14 to 16 g/dL.
• Whatever it may be, , the value varies depending upon the age and sex of the individual.
• 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
• At the time of birth, hemoglobin content is very high due to enhanced number of RBCs .
• SEX:-
• In adult males : 15 g/dL
• In adult females : 14.5 g/dL
• FUNCTIONAL ACTIVITIES OF HEMOGLOIBIN:-
• TRANSPORT OF RESPIRATORY GASES
• Main function of hemoglobin is the transport of respiratory gases:
• 1. Oxygen from the lungs to tissues.
• 2. Carbon dioxide from tissues to lungs.
• 1. TRANSPORT OF OXYGEN:_
• a) If oxygen binds with hemoglobin, a physical process termed as oxygenation happens, leading to
the formation of oxyhemoglobin.
• b)The iron remains in ferrous state in this compound.
• c) Oxyhemoglobin is an unstable compound and the combination is reversible, i.e. if more oxygen is
available, it binds with hemoglobin and whenever oxygen is needed, hemoglobin can release oxygen
readily .
• d)If oxygen is released from oxyhemoglobin, it is known as reduced hemoglobin or ferrohemoglobin.
• 2. TRANSPORT OF CARBON DIOXIDE:-
• a) If carbon dioxide binds with hemoglobin, the formation of carbhemoglobin takes place.
• b) It is also an unstable compound and the combination is reversible, i.e. the carbon dioxide can be
released from this compound
STRUCTURAL DIFFERENCE:-
a) In adult hemoglobin, the globin contains two α-chains and two β-chains.
b) In fetal hemoglobin, there are two α chains and two γ-chains instead of β-chains.
FUNCTIONAL DIFFERENCES:_
a)Regarding functional point of view, fetal hemoglobin exhibits more affinity for oxygen than that of
adult hemoglobin.
b)And, the oxygenhemoglobin dissociation curve of fetal blood is shifted to
left
• ABNORMAL HEMOGLOBIN:-
• Abnormal types of hemoglobin or hemoglobin variants are the pathologic mutant forms of
hemoglobin.
• The production of These variants occurs due to especially structural changes in the polypeptide
chains caused by mutation in the genes of the globin chains.
• Most of the mutations do not result in any serious problem. Occasionally, few mutations lead to
some disorders.
•
• There are two types of abnormal hemoglobin:
• 1. Hemoglobinopathies
• 2. Hemoglobin in thalassemia and related disorders.
• 1. HEMOGLOBINOPATHIES
• Hemoglobinopathy is a genetic disorder happened by abnormal polypeptide chains of hemoglobin. Some of the
hemoglobinopathies are:
•
• I. Hemoglobin S
• It is observed in sickle cell anemia. In this, the α-chains are normal and β-chains are abnormal.
• ii. Hemoglobin C
• The β-chains are abnormal. It is seen in people with hemoglobin C disease, which is manifested by mild hemolytic anemia as
well as splenomegaly.
• iii. Hemoglobin E:
• Here also the β-chains show abnormality. It is observed in people with hemoglobin E disease which is also manifested by mild
hemolytic anemia and splenomegaly.
• iv. Hemoglobin M:
• a)It is the abnormal hemoglobin present in the form of methemoglobin.
• b) It happens because of mutation of genes of both in α and β chains, leading to abnormal replacement of amino acids.
• c)It is seen in babies affected by hemoglobin M disease or blue baby syndrome. It is an inherited disease, manifested by
characterized by methemoglobinemia
• BUFFER FUNCTION:-
• Hemoglobin behaves as a buffer and plays an important role in acidbase balance.
• 
STRUCTURE OF HEMOGLOBIN
• Hemoglobin is a conjugated protein. It contains a protein combined with an ironcontaining pigment.
• The protein part is globin and the iron containing pigment is heme.
• Heme also forms a part of the structure of myoglobin (oxygen binding pigment in muscles) and neuroglobin (oxygen binding
pigment in brain)
• IRON:-
• Generally, it is seen in ferrous (Fe2+) form. It is in unstable or loose form.
• In some abnormal conditions, the iron is changed into ferric (Fe3+) state, which is a stable form.
•
• PORPHYRIN:-
• The pigment part of heme is ternmed as porphyrin. It is formed by four pyrrole rings (tetrapyrrole) termed as, I, II, III and IV.
• The pyrrole rings are bound to one another by methane (CH4 ) bridges. The iron is bound to ‘N’ of each pyrrole ring and ‘N’ of
globin molecule.
• GLOBIN:-
• Globin consists of four polypeptide chains. Among the four polypeptide chains, two are chains and two are α-chains
• TYPES OF NORMAL HEMOGLOBIB
• Hemoglobin is of two types:
• 1. Adult hemoglobin – HbA
• 2. Fetal hemoglobin – HbF
• Replacement of fetal hemoglobin by adult hemoglobin begins immediately after birth.
•
• SOURCES OF CABON MONOXIDE:-
• 1. Charcoal burning
• 2. Coal mines
• 3. Deep wells
• 4. Underground drainage system
• 5. Exhaust of gasoline engines
• 6. Gases from guns and other weapons
• 7. Heating system with poor or improper ventilation
• 8. Smoke from fire
• 9. Tobacco smoking
• SIGNS AND SYMPTOMS OF CARBON MONO OXIDE POISONING:-
•
• 1. While breathing air with less than 1% of CO, the Hb saturation is 15% to 20% and mild
symptoms like headache and nausea occur
•
• 2. While breathing air with more than 1% CO, the Hb saturation is 30% to 40%. It results in
severe symptoms such as:
• i. Convulsions
• ii. Cardio respiratory arrest
• iii. Unconsciousness and coma.
•
• When Hb saturation enhances above 50%, death occurs.
• METHMOGLOBIN:-
• Methemoglobin is the abnormal hemoglobin derivative formed if iron molecule of hemoglobin is
oxidized from normal ferrous state to ferric state. Methemoglobin
• is also termed as ferrihemoglobin.
• Normal methemoglobin level is 0.6% to 2.5% of total
• hemoglobin.
• Under normal circumstances also, body faces the threat of continuous production of
methemoglobin. But it is counteracted by erythrocyte protective system termed as nicotinamide
adenine dinucleotide (NADH) system, which operates with the help of two enzymes:
•
• 1. Diaphorase I (nicotinamide adenine dinucleotide phosphate [NADPH]dependent reductase):
Responsible for 95% of the action.
•
• Diaphorase II (NADPHdependent methemoglobin reductase): Responsible for 5% of the action.
• METHEMOGLOBINEMIA;_
• Methemoglobinemia is the disorder manifested by high level of methemoglobin in blood. It lresults
in tissue hypoxia, which causes cyanosis and other symptoms
• 2. HEMOGLOBIN IN THALASSEMIA AND RELATED DISORDERS:
•
• In thalassemia, different types of abnormal hemoglobins are observed. The polypeptide chains are
decreased, absent or abnormal.
• In α-thalassemia, the α-chains are decreased, absent or abnormal and in β-thalassemia, the β-
chains are decreased, absent or abnormal .
• Some of the abnormal hemoglobins found in thalassemia are hemoglobin G, H, I, Bart’s, Kenya,
Lepore and constant spring
• ABNORMAL HEMOGLOBIN DERIVATIVES
• ‘Hemoglobin derivatives’ refer to a blood test to identifyt and measure the percentage of abnormal hemoglobin derivatives.
• Hemoglobin is the only carrier particularly for transport of oxygen, without which tissue death happens within few minutes.
• When hemoglobin is altered, its oxygen carrying capacity is reduced leading to lack of oxygen. So, it is important to know about the causes and the effects of
abnormal hemoglobin derivatives.
• Abnormal hemoglobin derivatives are formed by carbon monoxide (CO) poisoning or due to some drugs like nitrites, nitrates and sulphanamides.
• ABNORMAL HEMOGLOBIN DERIVATIVES INCLUDE:-
•
• 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).
• Abnormally high levels of hemoglobin derivates in blood lead to serious effects. These derivatives inhibit the transport of oxygen resulting in oxygen lack in tissues,
which may be fatal
• CARBOXY HEMOGLOBIN:-
• a)Carboxyhemoglobin or carbon monoxyhemoglobin is the abnormal hemoglobin derivative formed by the combination of carbon monoxide along with hemoglobin.
• b)Carbon monoxide is a colorless and odorless gas. Since hemoglobin has200 times more affinity for carbon monoxide than oxygen, it inhibits the transport of
oxygen leading to tissue hypoxia.
• c)Generally, 1% to 3% of hemoglobin is in the form of carboxyhemoglobin. 80 Section 2 t Blood and Body Fluids
• CAUSES OF METHEMOGLOBINEMIA:-
• Methemoglobinemia is influenced by variety of factors:
• 1. COMMON FACTORS OF DAILY LIFE:-
• i. Well water contaminated with nitrates and nitrites
• ii. Fires
• iii. Laundry ink
• iv. Match sticks and explosives
• v. Meat preservatives (which contain nitrates and
• nitrites)
• vi. Mothballs (naphthalene balls)
• vii. Room deodorizer propellants.
•
• 2. EXPOSURE TO INDUSTRIAL CHEMICALS NAMELY:-
• i. Aromatic amines
• ii. Fluorides
• iii. Irritant gases like nitrous oxide and nitrobenzene
• iv. Propylene glycol dinitrate
• 3.DRUGS;-
• i. Antibacterial drugs namely sulfonamides
• ii. Antimalarial drugsnamely chloroquine
• iii. Antiseptics
• iv. Inhalant in cyanide antidote kit
• v. Local anesthetics namely benzocaine.
•
• 4. HEREDITARY TRAIT:-:
• a)Because of deficiency of NADH-dependant reductase or presence of abnormal hemoglobin M.
• b)Hemoglobin M is common in babies influenced by blue baby syndrome (a pathological condition
in infants, manifested by bluish skin discoloration (cyanosis), caused by congenital heart
• defect)
• BLOOD LEVEL OF SULFEHEMOGLOBIN:-
• Generally, very negligible amount of sulfhemoglobin is observed in blood which is nondetectable.
But when its level rises above 10 gm/dL, cyanosis happens Normally, serious toxic effects are not
observed..
• SYNTHESIS OF HEMOGLOBIN-
• Synthesis of hemoglobin actually begins within proerythroblastic stage . Whatever it may be ,
hemoglobin appears in the intermediate normoblastic stage only.
b)Continuation of the production of hemoglobin happens until the stage of reticulocyte.
• c) Heme portion of hemoglobin is synthesized in mitochondria and the protein part, globin is
synthesized in ribosomes
• SYNTHESIS OF HEME:-
• Heme is synthesized from succinylCoA and the glycine. The sequence of events in synthesis of hemoglobin:
•
• 1. First step in heme synthesis happens in the mitochondrion. Two molecules of succinylCoA bind with two molecules of glycine and
condense to form δ-aminolevulinic acid (ALA) by ALA synthase.
•
• 2. ALA is transported to the cytoplasm. Two molecules of ALA combine to form porphobilinogen in the presence of ALA dehydratase.
•
• 3. Porphobilinogen is converted into uroporphobilinogen I by uroporphobilinogen I synthase.
•
• 4. Uroporphobilinogen I is converted into uropor phobilinogen III by porphobilinogen III cosynthase.
•
• 5. From uroporphobilinogen III, a ring structure termed as coproporphyrinogen III is formed by
• Particulary uroporphobilinogen decarboxylase.
•
• 6. Coproporphyrinogen III is transported back to the mitochondrion, where it is oxidized to form protoporphyrinogen IX by
coproporphyrinogen oxidase
•
• 7. Protoporphyrinogen IX is converted into protoporphyrin IX by protoporphyrinogen oxidase.
•
• 8. Protoporphyrin IX combines with iron to form heme especially in the presence of ferrochelatase
• FORMATION OF GLOBIN:-
• The production of Polypeptide chains of globin occurs in in the ribosomes. b)There
are four types of polypeptide chains such as, alpha, beta, gamma and delta chains.
• Each of these chains differs from others because of the amino acid sequence. The formatioon of
each globin molecule occurs by the combination of 2 pairs of chains and each chain I consists of
141 to 146 amino acids.
• Adult hemoglobin consists of two alpha chains and two beta chains. Fetal hemoglobin consists of
two alpha chains and two gamma chains
• DESTRUCTION OF HEMOGLOBIN:-
• a)After the lifespan of 120 days, the RBC is demolished especially in the reticuloendothelial
system, particularly in spleen and the hemoglobin is released into plasma.
• b)Soon, the hemoglobin is deteriorated in the reticuloendothelial cells and divide into globin and
heme.
• c)Globin is utilized for the resynthesis of hemoglobin. Heme is degraded into iron and porphyrin.
• d) Iron is stored in the body as ferritin and hemosiderin, which are reutilized for the synthesis of new
hemoglobin.
• e)Porphyrin is changed into a green pigment called biliverdin. In human being, most of the
biliverdin is changed into a yellow pigment called bilirubin. Bilirubin and biliverdin are together
called the bile pigments
• References
• Hafen BB, Sharma S. StatPearls [Internet]. StatPearls
Publishing; Treasure Island (FL): Nov 23, 2022. Oxygen
Saturation. [PubMed]2. Chiabrando D, Mercurio S,
Tolosano E. Heme and erythropoieis: more than a
structural role. Haematologica. 2014 Jun;99(6):973-83.
[PMC free article] [PubMed]3. Harewood J, Azevedo
AM. StatPearls [Internet]. StatPearls Publishing;
Treasure Island (FL): Sep 4, 2023. Alpha Thalassemia.
[PubMed]4. Edel Y, Mamet R. Porphyria: What Is It
and Who Should Be Evaluated? Rambam Maimonides Med J.
2018 Apr 19;9(2) [PMC free article] [PubMed]5.
Farashi S, Harteveld CL. Molecular basis of α-
thalassemia. Blood Cells Mol Dis. 2018 May;70:43-53.
[PubMed]6. Forget BG, Bunn HF. Classification of
the disorders of hemoglobin. Cold Spring Harb Perspect
Med. 2013 Feb 01;3(2):a011684. [PMC free article]
[PubMed]7. Needs T, Gonzalez-Mosquera LF, Lynch DT.
StatPearls [Internet]. StatPearls Publishing; Treasure
Island (FL): May 1, 2023. Beta Thalassemia. [PubMed]8.

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Hemoglobin metabolism: C Kalyan & E. Muralinath

  • 2. • Hemoglobin (Hb) is the iron containing coloring material of red blood cell (RBC). It is a chromoprotein consisting of 95% of dry weight of RBC and 30% to 34% of wet weight. • Major activity of hemoglobin is to carry the respiratory gases, oxygen and carbon dioxide. It also behaves as a buffer. Molecular weight of hemoglobin is 68,000.
  • 3. • NORMAL HEMOGLOBIN CONTENT • Average hemoglobin (Hb) content in blood is 14 to 16 g/dL. • Whatever it may be, , the value varies depending upon the age and sex of the individual. • 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 • At the time of birth, hemoglobin content is very high due to enhanced number of RBCs . • SEX:- • In adult males : 15 g/dL • In adult females : 14.5 g/dL
  • 4. • FUNCTIONAL ACTIVITIES OF HEMOGLOIBIN:- • TRANSPORT OF RESPIRATORY GASES • Main function of hemoglobin is the transport of respiratory gases: • 1. Oxygen from the lungs to tissues. • 2. Carbon dioxide from tissues to lungs. • 1. TRANSPORT OF OXYGEN:_ • a) If oxygen binds with hemoglobin, a physical process termed as oxygenation happens, leading to the formation of oxyhemoglobin. • b)The iron remains in ferrous state in this compound. • c) Oxyhemoglobin is an unstable compound and the combination is reversible, i.e. if more oxygen is available, it binds with hemoglobin and whenever oxygen is needed, hemoglobin can release oxygen readily . • d)If oxygen is released from oxyhemoglobin, it is known as reduced hemoglobin or ferrohemoglobin.
  • 5. • 2. TRANSPORT OF CARBON DIOXIDE:- • a) If carbon dioxide binds with hemoglobin, the formation of carbhemoglobin takes place. • b) It is also an unstable compound and the combination is reversible, i.e. the carbon dioxide can be released from this compound STRUCTURAL DIFFERENCE:- a) In adult hemoglobin, the globin contains two α-chains and two β-chains. b) In fetal hemoglobin, there are two α chains and two γ-chains instead of β-chains. FUNCTIONAL DIFFERENCES:_ a)Regarding functional point of view, fetal hemoglobin exhibits more affinity for oxygen than that of adult hemoglobin. b)And, the oxygenhemoglobin dissociation curve of fetal blood is shifted to left
  • 6. • ABNORMAL HEMOGLOBIN:- • Abnormal types of hemoglobin or hemoglobin variants are the pathologic mutant forms of hemoglobin. • The production of These variants occurs due to especially structural changes in the polypeptide chains caused by mutation in the genes of the globin chains. • Most of the mutations do not result in any serious problem. Occasionally, few mutations lead to some disorders. • • There are two types of abnormal hemoglobin: • 1. Hemoglobinopathies • 2. Hemoglobin in thalassemia and related disorders.
  • 7. • 1. HEMOGLOBINOPATHIES • Hemoglobinopathy is a genetic disorder happened by abnormal polypeptide chains of hemoglobin. Some of the hemoglobinopathies are: • • I. Hemoglobin S • It is observed in sickle cell anemia. In this, the α-chains are normal and β-chains are abnormal. • ii. Hemoglobin C • The β-chains are abnormal. It is seen in people with hemoglobin C disease, which is manifested by mild hemolytic anemia as well as splenomegaly. • iii. Hemoglobin E: • Here also the β-chains show abnormality. It is observed in people with hemoglobin E disease which is also manifested by mild hemolytic anemia and splenomegaly. • iv. Hemoglobin M: • a)It is the abnormal hemoglobin present in the form of methemoglobin. • b) It happens because of mutation of genes of both in α and β chains, leading to abnormal replacement of amino acids. • c)It is seen in babies affected by hemoglobin M disease or blue baby syndrome. It is an inherited disease, manifested by characterized by methemoglobinemia
  • 8. • BUFFER FUNCTION:- • Hemoglobin behaves as a buffer and plays an important role in acidbase balance. •  STRUCTURE OF HEMOGLOBIN • Hemoglobin is a conjugated protein. It contains a protein combined with an ironcontaining pigment. • The protein part is globin and the iron containing pigment is heme. • Heme also forms a part of the structure of myoglobin (oxygen binding pigment in muscles) and neuroglobin (oxygen binding pigment in brain) • IRON:- • Generally, it is seen in ferrous (Fe2+) form. It is in unstable or loose form. • In some abnormal conditions, the iron is changed into ferric (Fe3+) state, which is a stable form. • • PORPHYRIN:- • The pigment part of heme is ternmed as porphyrin. It is formed by four pyrrole rings (tetrapyrrole) termed as, I, II, III and IV. • The pyrrole rings are bound to one another by methane (CH4 ) bridges. The iron is bound to ‘N’ of each pyrrole ring and ‘N’ of globin molecule. • GLOBIN:- • Globin consists of four polypeptide chains. Among the four polypeptide chains, two are chains and two are α-chains
  • 9. • TYPES OF NORMAL HEMOGLOBIB • Hemoglobin is of two types: • 1. Adult hemoglobin – HbA • 2. Fetal hemoglobin – HbF • Replacement of fetal hemoglobin by adult hemoglobin begins immediately after birth. • • SOURCES OF CABON MONOXIDE:- • 1. Charcoal burning • 2. Coal mines • 3. Deep wells • 4. Underground drainage system • 5. Exhaust of gasoline engines • 6. Gases from guns and other weapons • 7. Heating system with poor or improper ventilation • 8. Smoke from fire • 9. Tobacco smoking
  • 10. • SIGNS AND SYMPTOMS OF CARBON MONO OXIDE POISONING:- • • 1. While breathing air with less than 1% of CO, the Hb saturation is 15% to 20% and mild symptoms like headache and nausea occur • • 2. While breathing air with more than 1% CO, the Hb saturation is 30% to 40%. It results in severe symptoms such as: • i. Convulsions • ii. Cardio respiratory arrest • iii. Unconsciousness and coma. • • When Hb saturation enhances above 50%, death occurs.
  • 11. • METHMOGLOBIN:- • Methemoglobin is the abnormal hemoglobin derivative formed if iron molecule of hemoglobin is oxidized from normal ferrous state to ferric state. Methemoglobin • is also termed as ferrihemoglobin. • Normal methemoglobin level is 0.6% to 2.5% of total • hemoglobin. • Under normal circumstances also, body faces the threat of continuous production of methemoglobin. But it is counteracted by erythrocyte protective system termed as nicotinamide adenine dinucleotide (NADH) system, which operates with the help of two enzymes: • • 1. Diaphorase I (nicotinamide adenine dinucleotide phosphate [NADPH]dependent reductase): Responsible for 95% of the action. • • Diaphorase II (NADPHdependent methemoglobin reductase): Responsible for 5% of the action. • METHEMOGLOBINEMIA;_ • Methemoglobinemia is the disorder manifested by high level of methemoglobin in blood. It lresults in tissue hypoxia, which causes cyanosis and other symptoms
  • 12. • 2. HEMOGLOBIN IN THALASSEMIA AND RELATED DISORDERS: • • In thalassemia, different types of abnormal hemoglobins are observed. The polypeptide chains are decreased, absent or abnormal. • In α-thalassemia, the α-chains are decreased, absent or abnormal and in β-thalassemia, the β- chains are decreased, absent or abnormal . • Some of the abnormal hemoglobins found in thalassemia are hemoglobin G, H, I, Bart’s, Kenya, Lepore and constant spring
  • 13. • ABNORMAL HEMOGLOBIN DERIVATIVES • ‘Hemoglobin derivatives’ refer to a blood test to identifyt and measure the percentage of abnormal hemoglobin derivatives. • Hemoglobin is the only carrier particularly for transport of oxygen, without which tissue death happens within few minutes. • When hemoglobin is altered, its oxygen carrying capacity is reduced leading to lack of oxygen. So, it is important to know about the causes and the effects of abnormal hemoglobin derivatives. • Abnormal hemoglobin derivatives are formed by carbon monoxide (CO) poisoning or due to some drugs like nitrites, nitrates and sulphanamides. • ABNORMAL HEMOGLOBIN DERIVATIVES INCLUDE:- • • 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). • Abnormally high levels of hemoglobin derivates in blood lead to serious effects. These derivatives inhibit the transport of oxygen resulting in oxygen lack in tissues, which may be fatal
  • 14. • CARBOXY HEMOGLOBIN:- • a)Carboxyhemoglobin or carbon monoxyhemoglobin is the abnormal hemoglobin derivative formed by the combination of carbon monoxide along with hemoglobin. • b)Carbon monoxide is a colorless and odorless gas. Since hemoglobin has200 times more affinity for carbon monoxide than oxygen, it inhibits the transport of oxygen leading to tissue hypoxia. • c)Generally, 1% to 3% of hemoglobin is in the form of carboxyhemoglobin. 80 Section 2 t Blood and Body Fluids • CAUSES OF METHEMOGLOBINEMIA:- • Methemoglobinemia is influenced by variety of factors: • 1. COMMON FACTORS OF DAILY LIFE:- • i. Well water contaminated with nitrates and nitrites • ii. Fires • iii. Laundry ink • iv. Match sticks and explosives • v. Meat preservatives (which contain nitrates and • nitrites) • vi. Mothballs (naphthalene balls) • vii. Room deodorizer propellants. • • 2. EXPOSURE TO INDUSTRIAL CHEMICALS NAMELY:- • i. Aromatic amines • ii. Fluorides • iii. Irritant gases like nitrous oxide and nitrobenzene • iv. Propylene glycol dinitrate
  • 15. • 3.DRUGS;- • i. Antibacterial drugs namely sulfonamides • ii. Antimalarial drugsnamely chloroquine • iii. Antiseptics • iv. Inhalant in cyanide antidote kit • v. Local anesthetics namely benzocaine. • • 4. HEREDITARY TRAIT:-: • a)Because of deficiency of NADH-dependant reductase or presence of abnormal hemoglobin M. • b)Hemoglobin M is common in babies influenced by blue baby syndrome (a pathological condition in infants, manifested by bluish skin discoloration (cyanosis), caused by congenital heart • defect)
  • 16. • BLOOD LEVEL OF SULFEHEMOGLOBIN:- • Generally, very negligible amount of sulfhemoglobin is observed in blood which is nondetectable. But when its level rises above 10 gm/dL, cyanosis happens Normally, serious toxic effects are not observed.. • SYNTHESIS OF HEMOGLOBIN- • Synthesis of hemoglobin actually begins within proerythroblastic stage . Whatever it may be , hemoglobin appears in the intermediate normoblastic stage only. b)Continuation of the production of hemoglobin happens until the stage of reticulocyte. • c) Heme portion of hemoglobin is synthesized in mitochondria and the protein part, globin is synthesized in ribosomes
  • 17. • SYNTHESIS OF HEME:- • Heme is synthesized from succinylCoA and the glycine. The sequence of events in synthesis of hemoglobin: • • 1. First step in heme synthesis happens in the mitochondrion. Two molecules of succinylCoA bind with two molecules of glycine and condense to form δ-aminolevulinic acid (ALA) by ALA synthase. • • 2. ALA is transported to the cytoplasm. Two molecules of ALA combine to form porphobilinogen in the presence of ALA dehydratase. • • 3. Porphobilinogen is converted into uroporphobilinogen I by uroporphobilinogen I synthase. • • 4. Uroporphobilinogen I is converted into uropor phobilinogen III by porphobilinogen III cosynthase. • • 5. From uroporphobilinogen III, a ring structure termed as coproporphyrinogen III is formed by • Particulary uroporphobilinogen decarboxylase. • • 6. Coproporphyrinogen III is transported back to the mitochondrion, where it is oxidized to form protoporphyrinogen IX by coproporphyrinogen oxidase • • 7. Protoporphyrinogen IX is converted into protoporphyrin IX by protoporphyrinogen oxidase. • • 8. Protoporphyrin IX combines with iron to form heme especially in the presence of ferrochelatase
  • 18. • FORMATION OF GLOBIN:- • The production of Polypeptide chains of globin occurs in in the ribosomes. b)There are four types of polypeptide chains such as, alpha, beta, gamma and delta chains. • Each of these chains differs from others because of the amino acid sequence. The formatioon of each globin molecule occurs by the combination of 2 pairs of chains and each chain I consists of 141 to 146 amino acids. • Adult hemoglobin consists of two alpha chains and two beta chains. Fetal hemoglobin consists of two alpha chains and two gamma chains
  • 19.
  • 20. • DESTRUCTION OF HEMOGLOBIN:- • a)After the lifespan of 120 days, the RBC is demolished especially in the reticuloendothelial system, particularly in spleen and the hemoglobin is released into plasma. • b)Soon, the hemoglobin is deteriorated in the reticuloendothelial cells and divide into globin and heme. • c)Globin is utilized for the resynthesis of hemoglobin. Heme is degraded into iron and porphyrin. • d) Iron is stored in the body as ferritin and hemosiderin, which are reutilized for the synthesis of new hemoglobin. • e)Porphyrin is changed into a green pigment called biliverdin. In human being, most of the biliverdin is changed into a yellow pigment called bilirubin. Bilirubin and biliverdin are together called the bile pigments
  • 21. • References • Hafen BB, Sharma S. StatPearls [Internet]. StatPearls Publishing; Treasure Island (FL): Nov 23, 2022. Oxygen Saturation. [PubMed]2. Chiabrando D, Mercurio S, Tolosano E. Heme and erythropoieis: more than a structural role. Haematologica. 2014 Jun;99(6):973-83. [PMC free article] [PubMed]3. Harewood J, Azevedo AM. StatPearls [Internet]. StatPearls Publishing; Treasure Island (FL): Sep 4, 2023. Alpha Thalassemia. [PubMed]4. Edel Y, Mamet R. Porphyria: What Is It and Who Should Be Evaluated? Rambam Maimonides Med J. 2018 Apr 19;9(2) [PMC free article] [PubMed]5. Farashi S, Harteveld CL. Molecular basis of α- thalassemia. Blood Cells Mol Dis. 2018 May;70:43-53. [PubMed]6. Forget BG, Bunn HF. Classification of the disorders of hemoglobin. Cold Spring Harb Perspect Med. 2013 Feb 01;3(2):a011684. [PMC free article] [PubMed]7. Needs T, Gonzalez-Mosquera LF, Lynch DT. StatPearls [Internet]. StatPearls Publishing; Treasure Island (FL): May 1, 2023. Beta Thalassemia. [PubMed]8.