Sickle cell anemia is caused by a point mutation where glutamic acid is replaced by valine in the beta chain of hemoglobin, resulting in hemoglobin S (HbS) instead of normal hemoglobin A (HbA). Treatment options include hydroxyurea and bone marrow transplant. Myoglobin is a protein found in striated muscle that has a higher affinity for oxygen than hemoglobin. It may act as an intermediary to transfer oxygen from blood to mitochondria in muscle cells. It also functions to store oxygen in cardiac muscle. The chloride shift is a mechanism where chloride ions move into and out of red blood cells to help load oxygen onto hemoglobin in the lungs and unload it into

1. Inherited defects in haemoglobin
structure and function

2. 1. Sickel cell Anaemia :
• Hb-S instead of Hb-A
• Glutamic acid is replaced by valine

3. Drug – hydroxyurea
Bone marrow transplant

4. Causes
By over 200 different point
mutation in DNA
By rare DNA deletions

6. • Red pigment found exclusively in
striated muscle.
• Slow-twitch skeletal fibers and
cardiac muscle cells are rich in
myoglobin.
• Have a higher affinity for 02
than hemoglobin.
• May act as a “go-between” in
the transfer of 02 from blood
to the mitochondria within
muscle cells.
 May also have an 02 storage
function in cardiac muscles.
Muscle Myoglobin

8. Chloride Shift at Systemic Capillaries
• H20 + C02 H2C03 H+ + HC03
-
• At the tissues, C02 diffuses into the RBC; shifts the reaction
to the right.
• Increased [HC03
-] produced in RBC:
• HC03
- diffuses into the blood.
• RBC becomes more +.
• Cl- attracted in (Cl- shift).
• H+ released buffered by combining with deoxyhemoglobin.
• HbC02 formed.
• Unloading of 02.

9. The Reverse chloride shift
• H20 + C02 H2C03 H+ + HC03
-
• At the alveoli, C02 diffuses into the alveoli; reaction shifts
to the left.
• Decreased [HC03
-] in RBC, HC03
- diffuses into the RBC.
• RBC becomes more -.
• Cl- diffuses out (reverse Cl- shift).
• Deoxyhemoglobin converted to oxyhemoglobin.
• Has weak affinity for H+.
• Gives off HbC02