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Seminar physiopath

On the Hemoglobin pathophysiology

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12 views20 pages

Seminar physiopath

On the Hemoglobin pathophysiology

Uploaded by

sarthakkandwal2210
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd
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Effect On Oxygen

Binding
By-Atharva Pratap Singh Ran
Roll no - 28
Topics
• Binding of Oxygen to Hemoglobin

• Bohr Effect

• Types of Hemoglobin

• Abnormal Hemoglobin
Types Of Hemoglobin
• HbA1
⍺2ß2 chain
90% of total Hb

• HbA2
⍺2𝛅2 chain
2% of total Hb
Contd…..
• HbF

Composed of ⍺2𝛾2
Less than 2%

• HbA1c (<5%)
Covalent binding of glucose (⍺2β2-glucose)
Diagnosis and monitoring of Diabetes mellitus
Form of Hemoglobin
• T-Form
Deoxy form of Hemoglobin
Hydrogen and ionic bond limit monomer movement.

• R-Form
Oxygen destabilizes hydrogen and ionic bonds of ⍺β dimer
Resulting in a subunit having free movement
Binding Of Hemoglobin
• One molecule of Hemoglobin
(with four heme) can bind with
four molecules of Oxygen.

• Myoglobin (with one heme) can


bind with only one molecule of
oxygen.
Transport Of Oxygen to Tissue

• Lungs have high concentration of O2 so hemoglobin is fully


saturated .

• Tissue have low concentration of O2 so oxyhemoglobin release


O2 for cellular respiration .

• This is often carried out by myoglobin.


Oxygen Dissociation Curve
• The oxygen dissociation curve (ODC) is a graph that shows
the relationship between the partial pressure of oxygen and
hemoglobin's saturation with oxygen.

• The curve is sigmoidal (S-shaped) due to cooperative


binding, where the binding of one oxygen molecule increases
the affinity for subsequent oxygen molecules.

• Normal blood with 15 g/dL of Hb can carry 20 mL of O2/dL of


blood.
Contd…
• At higher pO₂ (e.g., in the lungs), hemoglobin has a high
affinity for oxygen and becomes saturated.

• At lower pO₂ (e.g., in tissues), hemoglobin's affinity for


oxygen decreases, promoting oxygen release.
Contd….
• At high pO₂ (above 60 mmHg), the
curve indicate that hemoglobin
remains highly saturated with
oxygen, ensuring sufficient oxygen
transport.

• The steep portion of the curve (20-


40 mmHg ) corresponds to tissues,
where small drops in pO₂ cause
large oxygen unloading.
Factors affecting ODC
(1) Temperature

(2) pH

(3) Bohr effect

(4) Effect of 2,3-BPG.


Bohr’s Effect
• The binding of oxygen to hemoglobin decreases with
decrease in pH or when the hemoglobin is exposed to
increased partial pressure of CO2 (pCO2). This
phenomenon is known as Bohr effect.
Mechanism Of Bohr Effect
• Any increase in protons or lower pO2 shifts the equilibrium to the right to
produce deoxyhemoglobin as happens in the tissues.

• Any increase in pO2 or decrease in H+ shifts the equilibrium to the left,


which occur in lungs.

• When CO2 binds to hemoglobin produce carbamyl hemoglobin which


causes removal of proton from the terminal NH2 group and stabilizes Hb
in T form.

• When hemoglobin js oxygenated in lungs, CO2 is released as it binds


loosely with R-form of Hb.
Effect Of pH
• A low pH (acidic environment) shifts
the oxygen dissociation curve to the
right, indicating reduced hemoglobin
affinity for oxygen and facilitating
oxygen release to tissues.

• A high pH (alkaline environment)


shifts the curve to the left, indicating
increased hemoglobin affinity for
oxygen, promoting oxygen binding in
the lungs.
Effect Of Temperature
• Increased temperature shifts the
oxygen dissociation curve to the right,
reducing hemoglobin's affinity for
oxygen .

• Decreased temperature shifts the curve


to the left, increasing hemoglobin's
affinity for oxygen and favoring oxygen
binding.
Effect Of 2,3-BPG

• Mechanism of Action:

• 2,3-BPG binds to the beta chains of deoxygenated


hemoglobin, stabilizing the T-state and decrease
hemoglobin's oxygen-binding affinity.

• It does not bind to oxygenated hemoglobin, thus allowing


efficient oxygen uptake in the lungs.
Contd…..
• Curve Shift:

• Increased levels of 2,3-BPG shift the oxygen dissociation


curve to the right, promoting oxygen unloading.

• Decreased levels of 2,3-BPG shift the curve to the left,


increasing oxygen affinity.
Abnormal Hb
HbS
Present in sickle cell anaemia
Consist of 2⍺ and 2β
Valine is replaced by glutamic acid on 6th position in β chain

HbC
Contain 2⍺ and 2β
Glutamic acid is replaced by lysine on 6th postion in β chain
Contd…
HbD
Contain 2⍺ and 2β
Glutamine replaced by glutamate on 12th position of β chain

HbE
Glutamide replaced by lysine on 26th position of β chain
Thank You

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