Haemoglobin is an iron-containing protein in red blood cells that transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It is a tetramer composed of two alpha and two non-alpha subunits. In adults, normal haemoglobin is 96-98% HbA which contains two alpha and two beta subunits. Fetal haemoglobin contains two alpha and two gamma subunits and makes up a smaller percentage. Mutations in the beta globin gene can result in haemoglobinopathies like sickle cell anemia.
Hemoglubin is are carrier protein for oxygen and CO2. it a pigmented and globular protein present within the red blood cell, its structure, synthesis, and how it function in the transportation of oxygen and CO2 are given in this presentation
Hemoglubin is are carrier protein for oxygen and CO2. it a pigmented and globular protein present within the red blood cell, its structure, synthesis, and how it function in the transportation of oxygen and CO2 are given in this presentation
A comprehensive presentation on Hemoglobin chemistry for medical ,dental ,biotechnology ,Life sciences ,& pharmacology students. Presentation includes structure & functions of a normal hemoglobin molecule.Bohr's effect along with allosteric modulators of hemoglobin for oxygen transport are illustrated.Molecular changes ,types,diagnosis, Management & inheritance of Sickle cell anemia is described .Types , mutations involved ,diagnosis ,inhertance & Management of Thalassemia disease is presented here . Presentation also involves other hemoglobinopathies Hb C/D/E /Lepore/Wyane etc.Changes in oxygen carrying capacity of hemoglobin after formation of Carboxy Hemoglobin is illustrated . Formation of Meth-Hb in vivo & in vitro is described along with its genetic & diagnostic aspects.Unstable variants & chronic Heinz body anemia are described briefly .Text is supported by Google images.
• A blood group also called a Blood Type.
• Classification of blood is based on the presence or absence
of inherited antigenic substances on the surface of red blood
cells (RBCs).
• These antigens may be proteins, carbohydrates,
glycoproteins, or glycolipids, depending on the blood group
system.
A comprehensive presentation on Hemoglobin chemistry for medical ,dental ,biotechnology ,Life sciences ,& pharmacology students. Presentation includes structure & functions of a normal hemoglobin molecule.Bohr's effect along with allosteric modulators of hemoglobin for oxygen transport are illustrated.Molecular changes ,types,diagnosis, Management & inheritance of Sickle cell anemia is described .Types , mutations involved ,diagnosis ,inhertance & Management of Thalassemia disease is presented here . Presentation also involves other hemoglobinopathies Hb C/D/E /Lepore/Wyane etc.Changes in oxygen carrying capacity of hemoglobin after formation of Carboxy Hemoglobin is illustrated . Formation of Meth-Hb in vivo & in vitro is described along with its genetic & diagnostic aspects.Unstable variants & chronic Heinz body anemia are described briefly .Text is supported by Google images.
• A blood group also called a Blood Type.
• Classification of blood is based on the presence or absence
of inherited antigenic substances on the surface of red blood
cells (RBCs).
• These antigens may be proteins, carbohydrates,
glycoproteins, or glycolipids, depending on the blood group
system.
Hemoglobin and myoglobin are two important proteins involved in the transport...tekalignpawulose09
1. Hemoglobin:
• Hemoglobin is found in red blood cells and is responsible for carrying oxygen from the lungs to the tissues and organs of the body.
• It consists of four protein subunits, each containing a heme group with an iron atom that binds to oxygen.
• Hemoglobin also helps in the transport of carbon dioxide from tissues back to the lungs for exhalation.
• The function of hemoglobin is vital for the body's oxygen transport system and overall metabolism.
2. Myoglobin:
• Myoglobin is a protein found in muscle tissues and serves as an oxygen reservoir for muscle cells.
• It contains a single heme group that binds to oxygen, similar to hemoglobin.
• Myoglobin stores oxygen in muscle cells and releases it when needed, helping in the supply of oxygen during muscle activity.
• This protein helps muscles sustain aerobic metabolism and endurance during physical activities.
Hemoglobin is a protein molecule in red blood cells that carries oxygen from the lungs to the body's tissues and returns carbon dioxide from the tissues back to the lungs. It is made up of four heme groups, each bound to a globin protein chain. Hemoglobin plays a crucial role in maintaining the body's oxygen balance and is essential for overall health. Variations in hemoglobin levels can indicate different health conditions, such as anemia or dehydration.
Macromolecules of life (Nucleic acids & Proteins)Amany Elsayed
Macromolecules of life (Nucleic acids & Proteins)
The Fibrous Proteins
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HEMOGLOBIN - STRUCTURE IN RELATION TO FUNCTIONMuunda Mudenda
Hemoglobin (Haemoglobin) is one of the most widely studied proteins in biology. It also stands as the first protein to have been crystallized and its structure elucidated. Apart from that, hemoglobin gave scientists a better understanding of the structure to function phenomenon in proteomics. This document discusses hemoglobin including the types and mechanism of action in its roles of oxygen and carbon dioxide transportation. Please note that this document is for academic purposes and does not, in any way, claim to be exhaustive. However, if you would like to understand the subject in more depth, write me an email and we can discuss the subject together. Enjoy the read.
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APNIC Foundation, presented by Ellisha Heppner at the PNG DNS Forum 2024APNIC
Ellisha Heppner, Grant Management Lead, presented an update on APNIC Foundation to the PNG DNS Forum held from 6 to 10 May, 2024 in Port Moresby, Papua New Guinea.
Understanding User Behavior with Google Analytics.pdfSEO Article Boost
Unlocking the full potential of Google Analytics is crucial for understanding and optimizing your website’s performance. This guide dives deep into the essential aspects of Google Analytics, from analyzing traffic sources to understanding user demographics and tracking user engagement.
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Discover where your website traffic originates. By examining the Acquisition section, you can identify whether visitors come from organic search, paid campaigns, direct visits, social media, or referral links. This knowledge helps in refining marketing strategies and optimizing resource allocation.
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Gain a comprehensive view of your audience by exploring demographic data in the Audience section. Understand age, gender, and interests to tailor your marketing strategies effectively. Leverage this information to create personalized content and improve user engagement and conversion rates.
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Instagram has become one of the most popular social media platforms, allowing people to share photos, videos, and stories with their followers. Sometimes, though, you might want to view someone's story without them knowing.
Meet up Milano 14 _ Axpo Italia_ Migration from Mule3 (On-prem) to.pdfFlorence Consulting
Quattordicesimo Meetup di Milano, tenutosi a Milano il 23 Maggio 2024 dalle ore 17:00 alle ore 18:30 in presenza e da remoto.
Abbiamo parlato di come Axpo Italia S.p.A. ha ridotto il technical debt migrando le proprie APIs da Mule 3.9 a Mule 4.4 passando anche da on-premises a CloudHub 1.0.
4. Introduction
• The main function of red blood cell
Gas transport protein
• 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
• HbA: 2 α & 2 β with heme .
• Molecular weight :68000 or 64500 daltons
• Other haemoglobin :HbF & HbA2
5. Normally Found Hemoglobin
Adult Hb (Hb A) 2 α and 2 β subunits
•HbA1 is the major form of Hb in adults and in
children over 7 months.
•HbA2 (2 α, 2 δ) is a minor form of Hb in adults.
It forms only 2 – 3% of a total Hb A.
Fetal Hb (Hb F) = 2 α and 2 γ subunits
in fetus and newborn infant,
After birth, Hb F is replaced by Hb A during the
first few months of life.
6. Hb AHb A Hb AHb A22 Hb FHb F
structurestructure 22ββ22 2222 22γγ22
Normal %Normal % 96-98 %96-98 % 1.5-3.2 %1.5-3.2 % 0.5-0.8 %0.5-0.8 %
Adult haemoblobin
7. haemoglobin
• Is a haemoprotein only found in the cytoplasm of
erythrocytes (ery)
Normal concentration of Hb in the
blood:
adult males 13.5 – 17.5 g/dL
adult females 12 – 15 g/dL
10. haemoglobin
• haemoglobin is made from two similar
proteins that "stick together".
• Both proteins must be present for the
haemoglobin to pick up and release oxygen
normally.
• One of the component proteins is called α, the
other is β.
11. Haemoglobin
• Blood cells are made up of two components.
• The haemoglobin is inside the cell.
• The cell is surrounded by a membrane that
holds in the haemoglobin.
12. Structure of haemoglobin
Tetramer:
Haemoglobin is a tetramer composed of four Polypeptide chain
and four heme groups.
α chain consist of 141 Amino acids
β chains has 146 Amino acids
Helical :
Each polypeptide chain arrange in a helical structure.
There are eight helical segments designated A to H
Iron of heme is covalently bounds to histamine at Position F on
H Segment.
13. Heme
• Heme is suspended
in a pocket form by
the folding of the
poly peptide chain.
• The four Polypeptide
chain make contact
at α1β1 and α1β2
14. Iron and haemoglobin
• Iron, plays an important
role in the body’s
delivery and use of
oxygen to and by
working muscles.
• It binds oxygen to
haemoglobin, which
then travels in the
bloodstream to
locations throughout
the body.
15.
16. Function of haemoglobin
Hb is a buffer (Hb/Hb-H+
) in the
erythrocytes
Hb is a carrier of O2 and CO2
Binding of O2is a cooperative. Hb binds O2
weakly at low oxygen pressures and tightly at
high pressures. The binding of the first O2 to Hb
enhances the binding futher O2 molecules →
allosteric effect → S-shaped (sigmoidal)
saturation curve of Hb
19. Myoglobin (Mb)
• is a single-chain
globular protein of
153 AA, containing
1 heme group
• transports O2 in
skeletal and heart
muscle
• is found in cytosol
within cells
• is a marker of
myocard damage
20. Process of O2
binding to Hb
•Hb can exist in 2 different forms: T-form and R-form.
•T-form (T = „tense“) has a much lower oxygen affinity than
the R-form. The subunits of Hb are held together by electrostatic
interactions. The binding of the first O2molecule to subunit of the
T-form leads to a local conformational change that weakens the
association between the subunits → R-form („relaxed“) of Hb.
•Increasing of oxygen partial pressure causes the conversion
of T-form to R-form.
21. PROCESS OF O2
BINDING TO HB
• haemoglobin is a remarkable molecular
machine that uses motion and small structural
changes to regulate its action.
• Oxygen binding at the four heme sites in
haemoglobin does not happen
simultaneously.
• Once the first heme binds oxygen, it
introduces small changes in the structure of
the corresponding protein chain.
22. PROCESS OF O2
BINDING TO HB
• These changes nudge the neighboring chains
into a different shape, making them bind
oxygen more easily.
• Thus, it is difficult to add the first oxygen
molecule, but binding the second, third and
fourth oxygen molecules gets progressively
easier and easier.
• This provides a great advantage in
haemoglobin function.
23. PROCESS OF O2
BINDING TO HB
• When blood is in the lungs, where oxygen is
plenty, oxygen easily binds to the first subunit
and then quickly fills up the remaining ones.
• Then, as blood circulates through the body,
the oxygen level drops while that of carbon
dioxide increases.
24. PROCESS OF O2
BINDING TO HB
• In this environment, haemoglobin releases its
bound oxygen. As soon as the first oxygen
molecule drops off, the protein starts changing its
shape.
• This prompts the remaining three oxygens to be
quickly released.
• In this way, haemoglobin picks up the largest
possible load of oxygen in the lungs, and delivers
all of it where and when needed.
25. haemoglobin
The heme group of one subunit, shown in the little
circular window, is kept in one place so that you can see
how the protein moves around it when oxygen binds.
As it binds to the iron atom in the center of the heme, it
pulls a histidine amino acid upwards on the bottom side
of the heme.
This shifts the position of an entire α helix, This motion is
propagated throughout the protein chain and on to the
other chains, ultimately causing the large rocking
motion of the two subunits
26. Haem synthesis
• Haem consis of proporphyrin ring with an iron
atom at its center .The porphyrin ring consist
of four pyrole group,which are united by
methene =c= bridges.
28. Haem synthesis
• Haem is synthesized from precursor succinyl
CoA and glycine,which condensed to Delta
Amino Laevulinic acid.dALA in presence of
ALA synthetase and pyrodixal phosphate as co
enzymes.
31. Derivatives of haemoglobin
Oxyhaemoglobin (oxyHb) = Hb with O2
Deoxyhaemoglobin (deoxyHb) = Hb without O2
Methaemoglobin (metHb) contains Fe3+
instead of Fe2+
in heme groups
Carbonylhaemoglobin (HbCO) – CO binds to Fe2+
in heme in case of
CO poisoning or smoking. CO has 200x higher affinity to Fe2+
than O2.
Carbaminohaemoglobin (HbCO2) - CO2 is non-covalently bound to globin
chain of Hb. HbCO2 transports CO2 in blood (about 23%).
Glycohaemoglobin (HbA1c) is formed spontaneously by nonenzymatic
reaction with Glc. People with DM have more HbA1c than normal (› 7%).
Measurement of blood HbA1c is useful to get info about long-term
control of glycemia.
32. Mutations in haemoglobin (haemoglobinopathies:
1- Sickle cell anemia (Hb S disease):
It is a genetic disorder of blood caused by mutation in β-globin
chain resulting in the formation of Hb S. The mutation occurs in 6th
position of β-chain where glutamic acid is replaced by valine .
33. Such sickled cells frequently block flow of blood in narrow
capillaries and block blood supply to tissue (tissue anoxia)
causing pain and cell death.
Note: The lifetime of erythrocyte in sickle cell is less than 20
days, compared to 120 days for normal RBCs.
Patients may be :
Heterozygotes (Hb AS): mutation occurs only in one β-
globin chain. These patients have sickle cell trait with no
clinical symptoms and can have normal life span.
Homozygotes (Hb SS): mutation occurs in both β-globin
chain with apparent anemia and its symptoms
34. 2- Hb C disease:
Like HbS, Hb C is a mutant Hb in which
glutamic acid in 6th
position of β-chain is
replaced by lysine.
RBCs will be large oblong and hexagonal.
The heterozygous form (HbAC) is
asymptomatic.
The homozygous form (Hb CC) causes anemia,
tissue anoxia and severe pain.