Hemoglobin ppt. hemoglobin presentation, Hemoglobin short notes, What is hemoglobin, structure of hemoglobin, types of hemoglobin, hemoglobin test, hemoglobin disease Disease related to hemoglobin, hemoglobin increase, hemoglobin decrease, hemoglobin level, hemoglobin normal range Medical notes, Nursing notes, paramedical notes, hemoglobin paramedical notes, hemoglobin mbbs notes, hemoglobin nursing notes.

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3.  Hemoglobin (Hb) is a conjugated protein
present in red blood cells and it constitutes
more than 90% of the dry weight of these
cells.
 It transports oxygen from the lungs to the
tissues, and carbon dioxide from tissues to
the lungs.
 Hb also serves to destroy the nitric oxide
molecule, which is physiologically important.
 Oxygen affinity of Hb is an important
property of Hb.

4. Structure and Synthesis of Hb
 Hb is synthesized in the
precursors of red cells during
their development in the bone
marrow.
 It appears in the early
normoblast stage and attains
maximum concentration in the
late normoblast stage.

5. Structure
Hb is made up of heme and globin.
Heme
 Heme is a complex molecule made up of a
series of tetrapyrrole rings, terminating in
protoporphyrin, with a central iron atom.
 Following the destruction of red cells, the
components of hemoglobin undergo
metabolic degradation.
 The iron part of heme is recycled and used
up again in the hemoglobin synthesis.
 The only component of Hb that cannot be
recycled is protoporphyrin, which forms

6. Globin
 This is a protein substance that
consists of two pairs of polypeptide
chains.
 Each amino acid chain is attached to
a heme moiety to form a single
hemoglobin molecule.
 After the degradation of
hemoglobin, the globin component
breaks down into its amino acid
constituents that are recycled for
hemoglobin synthesis.

12. Hemoglobin A (Hb A)
 Hb A is the major Hb and comprises about 97% of the hemoglobin of adult
red cells.
 It consists of two alpha and two beta chains with the structural formula
(a2ß2).
 Hb A is detected in small amounts in the fetus as early as the eighth week
of intrauterine life.
 During the first few months of post-natal life, Hb A replaces Hb F and the
adult pattern is fully established in 6 months.

13. Haemoglobin A, (Hb A₂)
 This is the minor hemoglobin in the
adult red cells. It has the structural
formula of α2δ2.
 Hb A, is present in very small amounts at
birth and reaches the adult level of 3%
during the first year of life.
 Its concentration increases in some
anemias.

14. Fetal Hemoglobin (Hb F)
 Hb F is the major hemoglobin in intrauterine
life. It has the structural formula of α2γ2.
 Hb F accounts for 70 to 90% of hemoglobin at
term.
 It then falls rapidly to 25% in one month, and
5% in six months.
 Hb F concentra- tion in adults increases in
some types of anemia, hemoglo- binopathies,
and sometimes in leukemia.

15.  These hemoglobin are confined to very early stages of development.
 They are of 3 types.
 Hb Gower 1
 Hb Gower 2
 Hb Portland

16. Normal Values, Functions and
Variations
Normal Values
Adult males: 14 to 18 (16 ± 2) g/dL of blood
Adult females: 12 to 16 (14 ± 2) g/dL of blood
 In newborns, hemoglobin concentration is
normally16 to 22 g/dL, which occurs mainly due to
hemoconcentration.
 It decreases to 9 to 14 g/dL at about two to four
months of age.
 By ten years of age, the normal hemo globin
concentration will be 12 to 14 g/dL.

17. Functions of Hb
Hemoglobin serves three important functions.
1. It transports oxygen from lungs to the tissues by forming
oxyhemoglobin and carbon dioxide from tissues to lungs by
forming carbaminohemoglobin.
When fully saturated, 1g of hemoglobin carries 1.34 ml of
oxygen.
2.Hemoglobin acts as a buffer in maintaining blood.
3. Hb serves to destroy physiologically important nitric oxide molecule.
It imparts red color to the blood.
Erythrocytes look due to the presence of hemoglobin in them, which red pigment.

18. Conditions that Decrease Hb Concentration
Physiological
Children have values lower than that in adults and women have values lower than
that in males. Hb is less during pregnancy due to hemodilution.
Pathological
Hb is less in different types of anemia.
However, relative decrease in Hb concentration occurs in different pathological
conditions that produce hemodilution like excess ADH secretion as occurs in
pituitary tumors.

19.  Oxyhemoglobin
 Carboxyhemoglobin
 Carbaminohemoglobin
 Glycosylated hemoglobin
 Methemoglobin
 Nitrosohemoglobin

20.  When oxygen molecules combine with hemoglobin to transport oxygen
from lungs to tissues it form Oxyhemoglobin.
 When Hb combines with Carbon Monoxide it forms Carboxyhemoglobin
Hb has much greater affinity for CO than for Oxygen.
Formation of Carboxyhemoglobin is reversible.
 Binding of CO2 with Hb leads to formation of Carbaminohemoglobin.
It helps in transport of CO2 from tissues to lungs.

21. Conditions that Increase Hb
Concentration
Physiological
Hb level is high at high altitude that occurs due to hypoxia.
Hb is more in newborns.
In excessive sweating, relative increase in Hb occurs due to
hemoconcentration.
Pathological
Hb concentration increases in conditions that produce
hemoconcentration like severe diarrhea, vomiting etc; and
conditions that produce hypoxia like congenital heart disease,