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HB Structure & Function 2008

The document discusses the structure and function of hemoglobin, the protein in red blood cells that transports oxygen and carbon dioxide. It describes the subunits that make up hemoglobin, how it binds oxygen through the heme group, and how environmental factors like pH, carbon dioxide levels, and 2,3-DPG affect the oxygen dissociation curve and hemoglobin's affinity for oxygen.

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Rhomizal Mazali
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Download as PPT, PDF, TXT or read online on Scribd
54 views

HB Structure & Function 2008

The document discusses the structure and function of hemoglobin, the protein in red blood cells that transports oxygen and carbon dioxide. It describes the subunits that make up hemoglobin, how it binds oxygen through the heme group, and how environmental factors like pH, carbon dioxide levels, and 2,3-DPG affect the oxygen dissociation curve and hemoglobin's affinity for oxygen.

Uploaded by

Rhomizal Mazali
Copyright
© © All Rights Reserved
Available Formats
Download as PPT, PDF, TXT or read online on Scribd
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DEPT OH HAEMATOLOGY SCHOOL OF MEDICAL SCIENCES

Structure of Haemoglobins
The main function of red blood cell Transfer of O2 from lungs to tissue Transfer of CO2 from tissue to lungs To accomplish this function red cells has haemoglobin (Hb) Each red cell has 640 million molecules of Hb Haemoglobin (Hb), protein constituting 1/3 of the red blood cells

Structure of Haemoglobins
A red coloured protein pigment found within RBC's. Mol. Wt : 64,500 (-like and -like MW about 15,750 and 16,500 respectively) 400 variants of Hb been described

Structure of Haemoglobins
Same basic structure : haem group mediates reversible binding of O2 by Hb Fe2+ Four globin polypeptide chains -2 pairs of or -like and 2 pairs of non- - protein that surrounds & protect haem molecules

Structure of Haemoglobins
There are four haem-iron complexes, thus can bind four oxygen molecules. The structure changes slightly during the binding and release of oxygen. The forms are important for oxygen binding and release.

Structure of Haemoglobins
The bonds between 1 and 2 chains are weaker than, 1 and 1

1 and 2 able to move or twisted thus allowing for the change between the tense and relaxed forms of Hb

Normal Hb variants
3 months post conception (fetus life) Hb Portland (22), Gower 1 (22), Gower 2 (22) At birth : Hb F (22) (80%) , Hb A (22), Hb A2 (22) 1 years/adult : Hb A (22) (97%) , Hb A2 (22), Hb F (22)

Structural relations of globin, 2,3-DPG and Heme


HbA molecule with two and two chains

Central cavity is one molecule of 2,3-DPG bonded to chain in a non-oxygenated state 2,3-DPG is expelled in an oxygenated

Structural relations of globin, 2,3-DPG and Hemecont

Non-oxygenated Hb structure tense (T) form Beta chains of molecule move farther apart and the molecule binds 2,3-DPG The presence of 2,3-DPG in Hb encourages O2 delivery to tissue Oxygenated Hb structure relaxed (R) form 2,3-DPG is expelled and Hb takes on R form. Permits further O2 binding

Functions of Haemoglobin
Transport of O2 from lungs to the tissue Transport of CO2 from tissues to lung Buffering of blood

Functions of Haemoglobin
Oxygenation not oxidation
One Hb can bind to four O2 molecules chain move closer when oxygenated

When oxygenated 2,3-DPG is pushed out chains are pulled apart when O2 is unloaded, permitting entry of 2,3-DPG resulting in lower affinity of O2

Oxygen transport
The primary function of Hb is to transport oxygen from the lungs to tissues. Transport of oxygen is based on interaction between O2 and heme Oxygen affinity is affected by the phenomenon of hemeheme interaction. Each heme-globin unit has ability to bind to one O2 molecule. At anytime the Hb molecule may be carrying one, two, three or four O2 molecules.

Oxygen transportcont The Hb curves are sigmoid (S-shaped) compare to myoglobin , rectangular hyperbola.

This difference arises because Hb is allosteric and show cooperative oxygen binding kinetics, whereas myoglobin is not allosteric.
The binding of each molecule of oxygen to Hb causes binding of additional oxygen molecules, (this cooperativity is due to tetrameric structure of Hb). HbF holds oxygen tightly.

Oxy & deoxyhaemoglobin

Oxygen dissociation curve


The normal position of curve depends on
Concentration of 2,3-DPG H+ ion concentration (pH) CO2 in red blood cells Structure of Hb

Oxygen dissociation curve


Right shift (easy oxygen delivery)
High 2,3-DPG High H+ High CO2 HbS

Left shift (give up oxygen less readily)


Low 2,3-DPG HbF

Carbon dioxide transport


CO2 exerts an effect on HbO2 uptake and similar to the Bohr effect. In the tissues, increased blood CO2 levels Decreased Hb affinity to O2 ODC shift to the Encourages release of O2 and increases binding of CO2 thus removing it from the tissues. Blood containing nonoxygenated Hb has a greater affinity for CO2 than does oxygenated blood because of Bohr effect.

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