Hemoglobin is the main protein in red blood cells that carries oxygen from the lungs to tissues and returns carbon dioxide back to the lungs. It is composed of four globin chains, including two alpha and two beta chains, that bind to an iron-containing heme group. Hemoglobin synthesis begins in early red blood cells and continues through their maturation. In adults, each red blood cell contains over 600 million hemoglobin molecules to carry oxygen throughout the body before the cells are broken down after around 120 days. Alterations in hemoglobin structure can cause serious diseases like sickle cell anemia.
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.
Macromolecules of life (Nucleic acids & Proteins)Amany Elsayed
Macromolecules of life (Nucleic acids & Proteins)
The Fibrous Proteins
The Collagens
The Globular Proteins
Structure and Function of Myoglobin
Minor Hemoglobin’s
Biological value of proteins
Nitrogen Balance
Protein Deficiency
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.
Macromolecules of life (Nucleic acids & Proteins)Amany Elsayed
Macromolecules of life (Nucleic acids & Proteins)
The Fibrous Proteins
The Collagens
The Globular Proteins
Structure and Function of Myoglobin
Minor Hemoglobin’s
Biological value of proteins
Nitrogen Balance
Protein Deficiency
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.
complete information related to hemoglobin , its structure, functions etc.
oxygen - hemoglobin dissociation curve, items essential for the synthesis of hemoglobin , destruction of hemoglobin into heme & globin portion, abormal derivatives of hemoglobin .
iron its metabolism,absorption,storage etc is also given
applied physiology.
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.
complete information related to hemoglobin , its structure, functions etc.
oxygen - hemoglobin dissociation curve, items essential for the synthesis of hemoglobin , destruction of hemoglobin into heme & globin portion, abormal derivatives of hemoglobin .
iron its metabolism,absorption,storage etc is also given
applied physiology.
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.
Ethnobotany and Ethnopharmacology:
Ethnobotany in herbal drug evaluation,
Impact of Ethnobotany in traditional medicine,
New development in herbals,
Bio-prospecting tools for drug discovery,
Role of Ethnopharmacology in drug evaluation,
Reverse Pharmacology.
How to Split Bills in the Odoo 17 POS ModuleCeline George
Bills have a main role in point of sale procedure. It will help to track sales, handling payments and giving receipts to customers. Bill splitting also has an important role in POS. For example, If some friends come together for dinner and if they want to divide the bill then it is possible by POS bill splitting. This slide will show how to split bills in odoo 17 POS.
Unit 8 - Information and Communication Technology (Paper I).pdfThiyagu K
This slides describes the basic concepts of ICT, basics of Email, Emerging Technology and Digital Initiatives in Education. This presentations aligns with the UGC Paper I syllabus.
Read| The latest issue of The Challenger is here! We are thrilled to announce that our school paper has qualified for the NATIONAL SCHOOLS PRESS CONFERENCE (NSPC) 2024. Thank you for your unwavering support and trust. Dive into the stories that made us stand out!
Synthetic Fiber Construction in lab .pptxPavel ( NSTU)
Synthetic fiber production is a fascinating and complex field that blends chemistry, engineering, and environmental science. By understanding these aspects, students can gain a comprehensive view of synthetic fiber production, its impact on society and the environment, and the potential for future innovations. Synthetic fibers play a crucial role in modern society, impacting various aspects of daily life, industry, and the environment. ynthetic fibers are integral to modern life, offering a range of benefits from cost-effectiveness and versatility to innovative applications and performance characteristics. While they pose environmental challenges, ongoing research and development aim to create more sustainable and eco-friendly alternatives. Understanding the importance of synthetic fibers helps in appreciating their role in the economy, industry, and daily life, while also emphasizing the need for sustainable practices and innovation.
Students, digital devices and success - Andreas Schleicher - 27 May 2024..pptxEduSkills OECD
Andreas Schleicher presents at the OECD webinar ‘Digital devices in schools: detrimental distraction or secret to success?’ on 27 May 2024. The presentation was based on findings from PISA 2022 results and the webinar helped launch the PISA in Focus ‘Managing screen time: How to protect and equip students against distraction’ https://www.oecd-ilibrary.org/education/managing-screen-time_7c225af4-en and the OECD Education Policy Perspective ‘Students, digital devices and success’ can be found here - https://oe.cd/il/5yV
How to Make a Field invisible in Odoo 17Celine George
It is possible to hide or invisible some fields in odoo. Commonly using “invisible” attribute in the field definition to invisible the fields. This slide will show how to make a field invisible in odoo 17.
3. Four Hgb chains bind together loosely to form the entire
hemoglobin molecule. The different types of chains are
designated as
alpha (α)
beta (β)
(γ) gamma
(δ) delta chains.
4. • The synthesis of hemoglobin begins in the
proerythroblasts and continues even into the
reticulocyte stage of the RBCs.
5. ● Hemoglobin is the main protein in mature red blood
cells. Each RBC contains over 600 million hemoglobin
molecules. It is tetramer, that is, one molecule of
hemoglobin in adult is composed of four globin chains,
2 alpha and 2 beta. These chains are derived from
chromosome, mainly chromosome 16 and 11.
6.
7. ● It carries oxygen from the lungs, where blood is
oxygenated, to body cells. When saturated with oxygen,
hemoglobin is called oxyhemoglobin
8.
9. Carboxyhemoglobin
a compound formed in the blood by the binding of
carbon monoxide to hemoglobin. It is stable and
therefore cannot absorb or transport oxygen
13. in addition to oxygen and carbon dioxide, hemoglobin
takes up and releases a third gas, nitric oxide.
Nitric oxide plays an important role in regulating blood
pressure by relaxing the blood vessel walls, thus increasing
blood flow.
14. ● Hemoglobin is contained entirely in the red blood cells,
amounting to perhaps 35 percent of their weight.
● To combine properly with oxygen, red blood cells must
contain adequate hemoglobin.
● Hemoglobin, in turn, is dependent on iron for its formation.
● A deficiency of hemoglobin caused by a lack of iron in the
body leads to anemia.
15. ● Hemoglobin carries more than 20 times its volume of
oxygen. Some chemicals, such as carbon monoxide,
combine so firmly with hemoglobin that it can no longer
combine with oxygen.
16.
17.
18. ● After a life of perhaps 120 days, red blood cells are
destroyed in the spleen, or in the course of
circulation, their hemoglobin is broken into its
constituents, including iron, which enters new blood
cells formed in the bone marrow.
19.
20. ● When blood vessels rupture, as in an injury, the red cells
are released and escape into tissue, where they are
broken down. The hemoglobin is converted into bile
pigments, the color of which is responsible for the
appearance of bruises.
21.
22. ● Alterations in the structure of hemoglobin can lead to
life-threatening illnesses. The most important of these
conditions is sickle-cell anemia, which involves a
hereditary change in one of the amino acids that make
up hemoglobin. The thalassemia's are a group of
hereditary diseases of similar origin
● sickle cell anemia, the amino acid valine is substituted
for glutamic acid at one point in each of the two beta
chains. When this type of hemoglobin is exposed to low
oxygen, it forms elongated crystals inside the RBCs that
are sometimes 15 micrometers in length.)
23.
24.
25. ● Haemoglobin (Hb), protein constituting 1/3 of the red
blood cells
● Synthesis begins in proerythroblast
■ 65% at erythroblast stage
■ 35% at reticulocyte stage
● Two parts
■ Haem
■ Globin
26. ● Haem & globin produced at two different sites in the
cells
■Haem in mitochondria
■Globin in ribosome
27. HEMOGLOBIN FORMATION
the basic chemical steps in the formation of hemoglobin
First, succinyl-CoA, which is formed in the Krebs metabolic
cycle binds with glycine to form a pyrrole molecule.
In turn, four pyrroles combine to form protoporphyrin IX,
which then combines with iron to form the heme molecule.
Finally, each heme molecule combines with a long
polypeptide chain, a globin synthesized by ribosomes,
forming a subunit of hemoglobin called a hemoglobin
chain
28.
29. Each chain has a molecular weight of about 16,000; four
of these chains, in turn, bind together loosely to form the
whole hemoglobin molecule.
30. ● During the various stages of life such as embryonic, fetal and
adult stages, different globin chains are expressed. During the
fetal period, from about two months until birth, the dominant
globin chain is alpha and gamma and this is known as
fetal hemoglobin (HbF).
● However, shortly after birth about 3-6months, one will notice a
fall in fetal hemoglobin (HbF) and a there will be a rise in adult
hemoglobin (HbA). An alteration to the alpha or beta globin will
result in an abnormal hemoglobin.
31. FUNCTIONS
● The major role of hemoglobin is to carry oxygen from
the lungs to the tissues and return carbon dioxide (CO2)
from the tissue to the lungs. It is the oxygen carrying
component of RBCs. Oxygen binds to hemoglobin with
high affinity in an oxygen-rich environment and leaves
hemoglobin in an environment where there is not
enough oxygen.
32. Normal Range of Hb.
● For females the normal range for hemoglobin is : 11.5-
15.5 g/dl
● For males the normal range for hemoglobin is : 13.5-
17.5 g/dl
33. Conc of Hb in RBC
● RBCs can concentrate maximum Hb upto 34 gms per 100ML
Of Blood.
● OXYGEN BINDING POWER OF Hb:
MALE : 100 ml of Blood(16gm) can carry 21 ml of oxygen.
FEMALE : 100 ml of blood(14gms) can carry 19 ml of oxygen.
34. TYPES OF HAEMOGLOBIN
HbA ( Alpha2 Beta2)
HbA2 ( Alpha2 Delta2)
HbF ( Alpha2 Gamma2)
Gower I ( Zeta2 Epsilon 2)
Gower II (Alpha2 Epsilon2)