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 is the iron-containing protein in red blood cells that transports oxygen throughout the body. It is composed of four polypeptide chains and an iron-containing heme group. Normal hemoglobin levels vary based on age and sex. Hemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Abnormal hemoglobin variants can lead to conditions like sickle cell anemia and thalassemia. Red blood cells have an average lifespan of 120 days before being broken down, mainly in the spleen.
Title: Hemoglobin: The Oxygen-Carrying Marvel of Our Blood
Introduction:
Hemoglobin, a remarkable protein present in our red blood cells, plays a crucial role in maintaining our body's equilibrium. Its extraordinary ability to transport oxygen efficiently throughout the circulatory system ensures our survival and well-being. In this presentation, we will explore the fascinating world of hemoglobin, understanding its structure, function, and importance in sustaining human life.
Slide 1: What is Hemoglobin?
Hemoglobin, often represented as Hb, is a complex protein found in red blood cells (erythrocytes).
It is composed of four subunits, each carrying a heme group that binds to an oxygen molecule.
Slide 2: Structure of Hemoglobin
Display the 3D structure of hemoglobin, emphasizing the four globular subunits and heme groups.
Highlight the iron atom in each heme group, which is essential for oxygen binding.
Slide 3: Oxygen Binding
Describe how oxygen binds to the iron in the heme group, forming oxyhemoglobin.
Explain the cooperative binding nature of hemoglobin, where one oxygen molecule facilitates the binding of others.
Slide 4: Oxygen Release
Illustrate how hemoglobin releases oxygen in tissues with lower oxygen concentrations.
Discuss factors that influence oxygen release, such as pH and carbon dioxide levels.
Slide 5: Hemoglobin Variants
Introduce different hemoglobin variants, such as HbA, HbF, and HbS.
Briefly explain their unique properties and significance in various medical conditions.
Slide 6: Hemoglobin and Carbon Dioxide Transport
Explore how hemoglobin also aids in the transportation of carbon dioxide from tissues to the lungs.
Describe the formation of carbaminohemoglobin and its role in CO2 transport.
Slide 7: Hemoglobin Disorders
Highlight common hemoglobin disorders like anemia, sickle cell disease, and thalassemia.
Discuss their impact on overall health and the challenges faced by affected individuals.
Slide 8: Diagnostic and Clinical Applications
Showcase the clinical importance of hemoglobin analysis in diagnosing and monitoring various blood-related disorders.
Mention hemoglobin electrophoresis and other diagnostic techniques used in the assessment.
Slide 9: Regulation and Homeostasis
Explain how the body maintains a balance of hemoglobin levels to ensure optimal oxygen-carrying capacity.
Discuss the role of erythropoietin and iron metabolism in hemoglobin regulation.
Slide 10: Conclusion
Summarize the vital role of hemoglobin in transporting oxygen and maintaining physiological balance.
Emphasize the significance of understanding hemoglobin in clinical contexts and the advancement of medical treatments.
Hemoglobin is an iron-containing protein in red blood cells that carries oxygen and carbon dioxide throughout the body. It makes up about 30-34% of the wet weight of red blood cells. Hemoglobin is composed of protein globin and heme, which contains iron. In adults, hemoglobin levels are typically 14-16 g/dL. Hemoglobin transports oxygen as oxyhemoglobin and carbon dioxide as carbhemoglobin. It also acts as a buffer in the blood. There are two main types of hemoglobin - adult hemoglobin and fetal hemoglobin, which differs in structure and oxygen affinity. Abnormal hemoglobin can also occur due to genetic disorders or environmental factors. Iron is also important for hemoglobin synthesis and is
Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells. It transports oxygen from the lungs to the tissues and returns carbon dioxide from the tissues back to the lungs. Hemoglobin is a globular protein made up of four polypeptide subunits, with each subunit containing an embedded heme group that can bind one oxygen molecule. The binding of oxygen to hemoglobin is cooperative, meaning that the binding of the first oxygen molecule makes the other binding sites have a higher affinity for oxygen. This allows for efficient uptake and release of oxygen in the lungs and tissues respectively.
Hemoglobin is a protein in red blood cells that transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It is composed of four polypeptide chains and a heme group which binds oxygen. Hemoglobin has a cooperative binding of oxygen that allows it to efficiently deliver oxygen to tissues via an oxygen dissociation curve. Factors like pH, carbon dioxide levels, and 2,3-bisphosphoglycerate regulate hemoglobin's affinity for oxygen and facilitate unloading of oxygen in tissues.
Hemoglobin is an iron-containing protein in red blood cells that transports oxygen throughout the body. It is a tetramer made of two alpha and two beta globin chains, each with a heme group containing iron. Heme is synthesized from porphyrin and iron. Old red blood cells are broken down, liberating bilirubin from heme which is transported to the liver and excreted in bile and feces. Fetal hemoglobin differs slightly to facilitate oxygen transport to the fetus. Carbon dioxide is carried in the blood through dissolution, buffering by hemoglobin, and formation of carbaminohemoglobin.
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 is the iron-containing protein in red blood cells that transports oxygen throughout the body. It is composed of four polypeptide chains and an iron-containing heme group. Normal hemoglobin levels vary based on age and sex. Hemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Abnormal hemoglobin variants can lead to conditions like sickle cell anemia and thalassemia. Red blood cells have an average lifespan of 120 days before being broken down, mainly in the spleen.
Title: Hemoglobin: The Oxygen-Carrying Marvel of Our Blood
Introduction:
Hemoglobin, a remarkable protein present in our red blood cells, plays a crucial role in maintaining our body's equilibrium. Its extraordinary ability to transport oxygen efficiently throughout the circulatory system ensures our survival and well-being. In this presentation, we will explore the fascinating world of hemoglobin, understanding its structure, function, and importance in sustaining human life.
Slide 1: What is Hemoglobin?
Hemoglobin, often represented as Hb, is a complex protein found in red blood cells (erythrocytes).
It is composed of four subunits, each carrying a heme group that binds to an oxygen molecule.
Slide 2: Structure of Hemoglobin
Display the 3D structure of hemoglobin, emphasizing the four globular subunits and heme groups.
Highlight the iron atom in each heme group, which is essential for oxygen binding.
Slide 3: Oxygen Binding
Describe how oxygen binds to the iron in the heme group, forming oxyhemoglobin.
Explain the cooperative binding nature of hemoglobin, where one oxygen molecule facilitates the binding of others.
Slide 4: Oxygen Release
Illustrate how hemoglobin releases oxygen in tissues with lower oxygen concentrations.
Discuss factors that influence oxygen release, such as pH and carbon dioxide levels.
Slide 5: Hemoglobin Variants
Introduce different hemoglobin variants, such as HbA, HbF, and HbS.
Briefly explain their unique properties and significance in various medical conditions.
Slide 6: Hemoglobin and Carbon Dioxide Transport
Explore how hemoglobin also aids in the transportation of carbon dioxide from tissues to the lungs.
Describe the formation of carbaminohemoglobin and its role in CO2 transport.
Slide 7: Hemoglobin Disorders
Highlight common hemoglobin disorders like anemia, sickle cell disease, and thalassemia.
Discuss their impact on overall health and the challenges faced by affected individuals.
Slide 8: Diagnostic and Clinical Applications
Showcase the clinical importance of hemoglobin analysis in diagnosing and monitoring various blood-related disorders.
Mention hemoglobin electrophoresis and other diagnostic techniques used in the assessment.
Slide 9: Regulation and Homeostasis
Explain how the body maintains a balance of hemoglobin levels to ensure optimal oxygen-carrying capacity.
Discuss the role of erythropoietin and iron metabolism in hemoglobin regulation.
Slide 10: Conclusion
Summarize the vital role of hemoglobin in transporting oxygen and maintaining physiological balance.
Emphasize the significance of understanding hemoglobin in clinical contexts and the advancement of medical treatments.
Hemoglobin is an iron-containing protein in red blood cells that carries oxygen and carbon dioxide throughout the body. It makes up about 30-34% of the wet weight of red blood cells. Hemoglobin is composed of protein globin and heme, which contains iron. In adults, hemoglobin levels are typically 14-16 g/dL. Hemoglobin transports oxygen as oxyhemoglobin and carbon dioxide as carbhemoglobin. It also acts as a buffer in the blood. There are two main types of hemoglobin - adult hemoglobin and fetal hemoglobin, which differs in structure and oxygen affinity. Abnormal hemoglobin can also occur due to genetic disorders or environmental factors. Iron is also important for hemoglobin synthesis and is
Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells. It transports oxygen from the lungs to the tissues and returns carbon dioxide from the tissues back to the lungs. Hemoglobin is a globular protein made up of four polypeptide subunits, with each subunit containing an embedded heme group that can bind one oxygen molecule. The binding of oxygen to hemoglobin is cooperative, meaning that the binding of the first oxygen molecule makes the other binding sites have a higher affinity for oxygen. This allows for efficient uptake and release of oxygen in the lungs and tissues respectively.
Hemoglobin is a protein in red blood cells that transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It is composed of four polypeptide chains and a heme group which binds oxygen. Hemoglobin has a cooperative binding of oxygen that allows it to efficiently deliver oxygen to tissues via an oxygen dissociation curve. Factors like pH, carbon dioxide levels, and 2,3-bisphosphoglycerate regulate hemoglobin's affinity for oxygen and facilitate unloading of oxygen in tissues.
Hemoglobin is an iron-containing protein in red blood cells that transports oxygen throughout the body. It is a tetramer made of two alpha and two beta globin chains, each with a heme group containing iron. Heme is synthesized from porphyrin and iron. Old red blood cells are broken down, liberating bilirubin from heme which is transported to the liver and excreted in bile and feces. Fetal hemoglobin differs slightly to facilitate oxygen transport to the fetus. Carbon dioxide is carried in the blood through dissolution, buffering by hemoglobin, and formation of carbaminohemoglobin.
This document summarizes various hemoglobin derivatives and abnormalities. It discusses how carbon monoxide binds strongly to hemoglobin, preventing oxygen transport and causing poisoning. It also describes methemoglobin, which is formed when iron is oxidized in hemoglobin and cannot bind oxygen well. The document focuses on sickle cell anemia, explaining how a single amino acid substitution causes hemoglobin to polymerize and distort red blood cells into a sickle shape, leading to anemia, pain, and early death. Electrophoresis is used to diagnose abnormalities by comparing hemoglobin variant migration speeds.
This document discusses various hemoglobin derivatives that are formed due to ligands binding to the heme part of hemoglobin or changes in the iron oxidation state. It specifically describes carboxyhemoglobin which is formed when hemoglobin binds to carbon monoxide, preventing oxygen transport. Other derivatives discussed include methemoglobin and sulfhemoglobin. The document also examines hemoglobinopathies such as sickle cell anemia, caused by a single amino acid substitution, and thalassemias which involve impaired globin chain synthesis. Clinical manifestations and treatments for various hemoglobin derivatives and disorders are summarized.
Hemoglobin and myoglobin are oxygen-carrying proteins in the blood. Hemoglobin is a tetrameric protein composed of four polypeptide chains that carry oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Myoglobin is a single-chain protein that stores oxygen in muscle tissues. Both proteins use heme groups containing iron to reversibly bind oxygen. The binding of oxygen is influenced by factors like pH, carbon dioxide levels, and 2,3-bisphosphoglycerate to facilitate oxygen delivery to tissues and carbon dioxide removal from tissues.
Hemoglobin and myoglobin are hemoproteins that contain heme as a prosthetic group. Hemoglobin is found in red blood cells and transports oxygen from the lungs to tissues, as well as carbon dioxide in the reverse direction. It has a quaternary structure consisting of two alpha and two beta globin subunits noncovalently bound to a heme group. Myoglobin is found in muscle tissues and functions as an oxygen store. Hemoglobinopathies are genetic disorders caused by abnormalities in hemoglobin, the most common being sickle cell anemia caused by a mutation in the beta globin gene.
Haemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It exists as either oxygenated oxyhaemoglobin or deoxygenated haemoglobin. There are four main types of haemoglobin - embryonic, fetal, and two adult forms. Variants like haemoglobin S cause sickle cell disease. Laboratory tests like complete blood counts and blood smears evaluate red blood cells to diagnose haemoglobinopathies. Genetic testing identifies mutations in globin genes.
Structure Of Hemoglobin and Difference between Fetal and Adult Hemoglobin.Abdul Qadir Khan
Hemoglobin is the protein in red blood cells that carries oxygen from the lungs to tissues and carbon dioxide back to the lungs. Fetal hemoglobin differs from adult hemoglobin in its structure and oxygen affinity. Fetal hemoglobin is composed of two alpha and two gamma chains, has a shorter lifespan, and greater oxygen affinity to facilitate more oxygen delivery to the developing fetus. After birth, fetal hemoglobin production switches off and is replaced by over 90% adult hemoglobin composed of two alpha and two beta chains with lower oxygen affinity.
Hemoglobin is a protein in red blood cells that carries oxygen and carbon dioxide throughout the body. It is made up of a protein component called globin and an iron-containing component called heme. Heme gives blood its red color and allows hemoglobin to bind oxygen. Hemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. The breakdown of old red blood cells releases heme which is broken down to bilirubin in the liver and excreted in bile and feces. Elevated bilirubin levels can cause jaundice.
Hemoglobin is red color blood pigment, present in red blood cells (erythrocytes).
It is a chromoprotein, containing heme as the prosthetic group & globin as the protein part-apoprotein.
It is a tetrameric protein & molecular weight about 67,000 dalton.
Each gram of Hb contains 3.4 mg of iron.
Hemoglobin is the iron-containing protein in red blood cells that transports oxygen and carbon dioxide throughout the body. It consists of a protein component called globin and an iron-containing heme group. Hemoglobin exists in two forms - adult hemoglobin which contains two alpha and two beta chains, and fetal hemoglobin which contains two alpha and two gamma chains. Fetal hemoglobin has a higher affinity for oxygen to meet the needs of the developing fetus. Hemoglobin is synthesized through a series of steps involving the mitochondria and cytoplasm, where heme is produced from succinyl-CoA and glycine and globin chains are produced from the combination of alpha, beta, gamma and delta polypeptide chains in the ribosomes
This document discusses hemoglobin, its structure and types. It describes that hemoglobin is made up of heme and globin proteins, with each molecule containing two alpha globin chains and two non-alpha chains. The main types discussed are HbA, HbA2, HbF. Hemoglobinopathies and thalassemias are disorders involving abnormalities in hemoglobin structure or globin gene expression. Specific disorders covered include sickle cell anemia, sickle cell trait, hemoglobin H disease, Bart's hydrops fetalis, hereditary persistence of fetal hemoglobin and hemoglobin E.
This document summarizes the structure and types of hemoglobin and myoglobin. It discusses that hemoglobin is made up of globin and heme subunits that together form a tetrameric protein. There are different types of normal human hemoglobin, including adult and fetal hemoglobin which differ in their globin subunit composition. Hemoglobin can bind to ligands like oxygen to form derivatives such as oxyhemoglobin and carboxyhemoglobin. Myoglobin is a monomeric heme protein found in muscle that also binds oxygen, functioning as a local oxygen store.
Fish hemoglobin is similar to other vertebrate hemoglobin but has some key differences. It is a tetrameric molecule composed of two alpha and two beta globin chains, each containing a heme group. Unlike other vertebrates, fish hemoglobin has fewer histidine residues per globin chain and typically has serine instead of cysteine at position 93 of the beta chain. Fish hemoglobin also exists in multiple forms that differ in oxygen affinity and other properties. The heme group allows hemoglobin to reversibly bind oxygen, with factors like temperature, pH, salt concentrations, and partial pressures of oxygen and carbon dioxide impacting binding. Hemoglobin transports oxygen from gills to tissues via changes between tense and relaxed conformational states.
Hemoglobin variants are abnormal forms of hemoglobin that occur due to genetic changes in globin genes. Hemoglobin binds oxygen in the lungs and transports it throughout the body. There are three normal hemoglobin types - Hb A, Hb A2, and Hb F - which differ in their protein chain composition. Variant hemoglobin types can result from genetic changes to the globin genes. One common variant is hemoglobin S, which causes sickle cell disease and results in misshapen red blood cells that can block blood vessels.
Hemoglobin variants are abnormal forms of hemoglobin that occur due to genetic changes in globin genes. Hemoglobin binds oxygen in the lungs and transports it throughout the body. There are three normal hemoglobin types - Hb A, Hb A2, and Hb F - which differ in their protein chain composition. Variant hemoglobin types can result from genetic changes and one common variant is hemoglobin S, which causes sickle cell disease where red blood cells deform into a sickle shape, blocking blood vessels and reducing oxygen transport.
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.
1. Heme synthesis occurs in mitochondria and involves two starting molecules, succinyl CoA and glycine. The reaction produces aminolevulonic acid and needs the enzyme ALA synthase.
2. There are several types of hemoglobin in humans including HbA, HbA2, fetal Hb, and HbA1c. HbA1c levels are used to monitor diabetes by indicating average blood glucose levels over several weeks.
3. Abnormal hemoglobins include methemoglobin, carboxyhemoglobin, sulfhemoglobin, and hematin. Porphyrias are diseases caused by deficiencies in heme synthesis enzymes that can cause anemia, pain, and photosensitivity.
6) transport of oxygen and carbon dioxdideAyub Abdi
lecture 6: transportaion of both gases need a hemoglobin and part of them are transported by plasma. if Hb is low the saturation of oxygen also low and leads a hypoxia, fatigue, dyspnea, etc. in other hand acidosis can occur.
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 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.
This document summarizes various hemoglobin derivatives and abnormalities. It discusses how carbon monoxide binds strongly to hemoglobin, preventing oxygen transport and causing poisoning. It also describes methemoglobin, which is formed when iron is oxidized in hemoglobin and cannot bind oxygen well. The document focuses on sickle cell anemia, explaining how a single amino acid substitution causes hemoglobin to polymerize and distort red blood cells into a sickle shape, leading to anemia, pain, and early death. Electrophoresis is used to diagnose abnormalities by comparing hemoglobin variant migration speeds.
This document discusses various hemoglobin derivatives that are formed due to ligands binding to the heme part of hemoglobin or changes in the iron oxidation state. It specifically describes carboxyhemoglobin which is formed when hemoglobin binds to carbon monoxide, preventing oxygen transport. Other derivatives discussed include methemoglobin and sulfhemoglobin. The document also examines hemoglobinopathies such as sickle cell anemia, caused by a single amino acid substitution, and thalassemias which involve impaired globin chain synthesis. Clinical manifestations and treatments for various hemoglobin derivatives and disorders are summarized.
Hemoglobin and myoglobin are oxygen-carrying proteins in the blood. Hemoglobin is a tetrameric protein composed of four polypeptide chains that carry oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Myoglobin is a single-chain protein that stores oxygen in muscle tissues. Both proteins use heme groups containing iron to reversibly bind oxygen. The binding of oxygen is influenced by factors like pH, carbon dioxide levels, and 2,3-bisphosphoglycerate to facilitate oxygen delivery to tissues and carbon dioxide removal from tissues.
Hemoglobin and myoglobin are hemoproteins that contain heme as a prosthetic group. Hemoglobin is found in red blood cells and transports oxygen from the lungs to tissues, as well as carbon dioxide in the reverse direction. It has a quaternary structure consisting of two alpha and two beta globin subunits noncovalently bound to a heme group. Myoglobin is found in muscle tissues and functions as an oxygen store. Hemoglobinopathies are genetic disorders caused by abnormalities in hemoglobin, the most common being sickle cell anemia caused by a mutation in the beta globin gene.
Haemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It exists as either oxygenated oxyhaemoglobin or deoxygenated haemoglobin. There are four main types of haemoglobin - embryonic, fetal, and two adult forms. Variants like haemoglobin S cause sickle cell disease. Laboratory tests like complete blood counts and blood smears evaluate red blood cells to diagnose haemoglobinopathies. Genetic testing identifies mutations in globin genes.
Structure Of Hemoglobin and Difference between Fetal and Adult Hemoglobin.Abdul Qadir Khan
Hemoglobin is the protein in red blood cells that carries oxygen from the lungs to tissues and carbon dioxide back to the lungs. Fetal hemoglobin differs from adult hemoglobin in its structure and oxygen affinity. Fetal hemoglobin is composed of two alpha and two gamma chains, has a shorter lifespan, and greater oxygen affinity to facilitate more oxygen delivery to the developing fetus. After birth, fetal hemoglobin production switches off and is replaced by over 90% adult hemoglobin composed of two alpha and two beta chains with lower oxygen affinity.
Hemoglobin is a protein in red blood cells that carries oxygen and carbon dioxide throughout the body. It is made up of a protein component called globin and an iron-containing component called heme. Heme gives blood its red color and allows hemoglobin to bind oxygen. Hemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. The breakdown of old red blood cells releases heme which is broken down to bilirubin in the liver and excreted in bile and feces. Elevated bilirubin levels can cause jaundice.
Hemoglobin is red color blood pigment, present in red blood cells (erythrocytes).
It is a chromoprotein, containing heme as the prosthetic group & globin as the protein part-apoprotein.
It is a tetrameric protein & molecular weight about 67,000 dalton.
Each gram of Hb contains 3.4 mg of iron.
Hemoglobin is the iron-containing protein in red blood cells that transports oxygen and carbon dioxide throughout the body. It consists of a protein component called globin and an iron-containing heme group. Hemoglobin exists in two forms - adult hemoglobin which contains two alpha and two beta chains, and fetal hemoglobin which contains two alpha and two gamma chains. Fetal hemoglobin has a higher affinity for oxygen to meet the needs of the developing fetus. Hemoglobin is synthesized through a series of steps involving the mitochondria and cytoplasm, where heme is produced from succinyl-CoA and glycine and globin chains are produced from the combination of alpha, beta, gamma and delta polypeptide chains in the ribosomes
This document discusses hemoglobin, its structure and types. It describes that hemoglobin is made up of heme and globin proteins, with each molecule containing two alpha globin chains and two non-alpha chains. The main types discussed are HbA, HbA2, HbF. Hemoglobinopathies and thalassemias are disorders involving abnormalities in hemoglobin structure or globin gene expression. Specific disorders covered include sickle cell anemia, sickle cell trait, hemoglobin H disease, Bart's hydrops fetalis, hereditary persistence of fetal hemoglobin and hemoglobin E.
This document summarizes the structure and types of hemoglobin and myoglobin. It discusses that hemoglobin is made up of globin and heme subunits that together form a tetrameric protein. There are different types of normal human hemoglobin, including adult and fetal hemoglobin which differ in their globin subunit composition. Hemoglobin can bind to ligands like oxygen to form derivatives such as oxyhemoglobin and carboxyhemoglobin. Myoglobin is a monomeric heme protein found in muscle that also binds oxygen, functioning as a local oxygen store.
Fish hemoglobin is similar to other vertebrate hemoglobin but has some key differences. It is a tetrameric molecule composed of two alpha and two beta globin chains, each containing a heme group. Unlike other vertebrates, fish hemoglobin has fewer histidine residues per globin chain and typically has serine instead of cysteine at position 93 of the beta chain. Fish hemoglobin also exists in multiple forms that differ in oxygen affinity and other properties. The heme group allows hemoglobin to reversibly bind oxygen, with factors like temperature, pH, salt concentrations, and partial pressures of oxygen and carbon dioxide impacting binding. Hemoglobin transports oxygen from gills to tissues via changes between tense and relaxed conformational states.
Hemoglobin variants are abnormal forms of hemoglobin that occur due to genetic changes in globin genes. Hemoglobin binds oxygen in the lungs and transports it throughout the body. There are three normal hemoglobin types - Hb A, Hb A2, and Hb F - which differ in their protein chain composition. Variant hemoglobin types can result from genetic changes to the globin genes. One common variant is hemoglobin S, which causes sickle cell disease and results in misshapen red blood cells that can block blood vessels.
Hemoglobin variants are abnormal forms of hemoglobin that occur due to genetic changes in globin genes. Hemoglobin binds oxygen in the lungs and transports it throughout the body. There are three normal hemoglobin types - Hb A, Hb A2, and Hb F - which differ in their protein chain composition. Variant hemoglobin types can result from genetic changes and one common variant is hemoglobin S, which causes sickle cell disease where red blood cells deform into a sickle shape, blocking blood vessels and reducing oxygen transport.
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.
1. Heme synthesis occurs in mitochondria and involves two starting molecules, succinyl CoA and glycine. The reaction produces aminolevulonic acid and needs the enzyme ALA synthase.
2. There are several types of hemoglobin in humans including HbA, HbA2, fetal Hb, and HbA1c. HbA1c levels are used to monitor diabetes by indicating average blood glucose levels over several weeks.
3. Abnormal hemoglobins include methemoglobin, carboxyhemoglobin, sulfhemoglobin, and hematin. Porphyrias are diseases caused by deficiencies in heme synthesis enzymes that can cause anemia, pain, and photosensitivity.
6) transport of oxygen and carbon dioxdideAyub Abdi
lecture 6: transportaion of both gases need a hemoglobin and part of them are transported by plasma. if Hb is low the saturation of oxygen also low and leads a hypoxia, fatigue, dyspnea, etc. in other hand acidosis can occur.
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 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.
PPT on Alternate Wetting and Drying presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
PPT on Sustainable Land Management presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
PPT on Direct Seeded Rice presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...Creative-Biolabs
Neutralizing antibodies, pivotal in immune defense, specifically bind and inhibit viral pathogens, thereby playing a crucial role in protecting against and mitigating infectious diseases. In this slide, we will introduce what antibodies and neutralizing antibodies are, the production and regulation of neutralizing antibodies, their mechanisms of action, classification and applications, as well as the challenges they face.
TOPIC OF DISCUSSION: CENTRIFUGATION SLIDESHARE.pptxshubhijain836
Centrifugation is a powerful technique used in laboratories to separate components of a heterogeneous mixture based on their density. This process utilizes centrifugal force to rapidly spin samples, causing denser particles to migrate outward more quickly than lighter ones. As a result, distinct layers form within the sample tube, allowing for easy isolation and purification of target substances.
SDSS1335+0728: The awakening of a ∼ 106M⊙ black hole⋆Sérgio Sacani
Context. The early-type galaxy SDSS J133519.91+072807.4 (hereafter SDSS1335+0728), which had exhibited no prior optical variations during the preceding two decades, began showing significant nuclear variability in the Zwicky Transient Facility (ZTF) alert stream from December 2019 (as ZTF19acnskyy). This variability behaviour, coupled with the host-galaxy properties, suggests that SDSS1335+0728 hosts a ∼ 106M⊙ black hole (BH) that is currently in the process of ‘turning on’. Aims. We present a multi-wavelength photometric analysis and spectroscopic follow-up performed with the aim of better understanding the origin of the nuclear variations detected in SDSS1335+0728. Methods. We used archival photometry (from WISE, 2MASS, SDSS, GALEX, eROSITA) and spectroscopic data (from SDSS and LAMOST) to study the state of SDSS1335+0728 prior to December 2019, and new observations from Swift, SOAR/Goodman, VLT/X-shooter, and Keck/LRIS taken after its turn-on to characterise its current state. We analysed the variability of SDSS1335+0728 in the X-ray/UV/optical/mid-infrared range, modelled its spectral energy distribution prior to and after December 2019, and studied the evolution of its UV/optical spectra. Results. From our multi-wavelength photometric analysis, we find that: (a) since 2021, the UV flux (from Swift/UVOT observations) is four times brighter than the flux reported by GALEX in 2004; (b) since June 2022, the mid-infrared flux has risen more than two times, and the W1−W2 WISE colour has become redder; and (c) since February 2024, the source has begun showing X-ray emission. From our spectroscopic follow-up, we see that (i) the narrow emission line ratios are now consistent with a more energetic ionising continuum; (ii) broad emission lines are not detected; and (iii) the [OIII] line increased its flux ∼ 3.6 years after the first ZTF alert, which implies a relatively compact narrow-line-emitting region. Conclusions. We conclude that the variations observed in SDSS1335+0728 could be either explained by a ∼ 106M⊙ AGN that is just turning on or by an exotic tidal disruption event (TDE). If the former is true, SDSS1335+0728 is one of the strongest cases of an AGNobserved in the process of activating. If the latter were found to be the case, it would correspond to the longest and faintest TDE ever observed (or another class of still unknown nuclear transient). Future observations of SDSS1335+0728 are crucial to further understand its behaviour. Key words. galaxies: active– accretion, accretion discs– galaxies: individual: SDSS J133519.91+072807.4
Sexuality - Issues, Attitude and Behaviour - Applied Social Psychology - Psyc...PsychoTech Services
A proprietary approach developed by bringing together the best of learning theories from Psychology, design principles from the world of visualization, and pedagogical methods from over a decade of training experience, that enables you to: Learn better, faster!
2. • Hemoglobin (Hb) is the iron containing coloring material of red blood cell (RBC). It is a
chromoprotein consisting of 95% of dry weight of RBC and 30% to 34% of wet weight.
• Major activity of hemoglobin is to carry the respiratory gases, oxygen and carbon dioxide. It also
behaves as a buffer. Molecular weight of hemoglobin is 68,000.
3. • NORMAL HEMOGLOBIN CONTENT
• Average hemoglobin (Hb) content in blood is 14 to 16 g/dL.
• Whatever it may be, , the value varies depending upon the age and sex of the individual.
• AGE:-
• At birth 25 g/dL
• After 3rd month : 20 g/dL
• After 1 year 17 g/dL
• From puberty onwards : 14 to 16 g/dL
• At the time of birth, hemoglobin content is very high due to enhanced number of RBCs .
• SEX:-
• In adult males : 15 g/dL
• In adult females : 14.5 g/dL
4. • FUNCTIONAL ACTIVITIES OF HEMOGLOIBIN:-
• TRANSPORT OF RESPIRATORY GASES
• Main function of hemoglobin is the transport of respiratory gases:
• 1. Oxygen from the lungs to tissues.
• 2. Carbon dioxide from tissues to lungs.
• 1. TRANSPORT OF OXYGEN:_
• a) If oxygen binds with hemoglobin, a physical process termed as oxygenation happens, leading to
the formation of oxyhemoglobin.
• b)The iron remains in ferrous state in this compound.
• c) Oxyhemoglobin is an unstable compound and the combination is reversible, i.e. if more oxygen is
available, it binds with hemoglobin and whenever oxygen is needed, hemoglobin can release oxygen
readily .
• d)If oxygen is released from oxyhemoglobin, it is known as reduced hemoglobin or ferrohemoglobin.
5. • 2. TRANSPORT OF CARBON DIOXIDE:-
• a) If carbon dioxide binds with hemoglobin, the formation of carbhemoglobin takes place.
• b) It is also an unstable compound and the combination is reversible, i.e. the carbon dioxide can be
released from this compound
STRUCTURAL DIFFERENCE:-
a) In adult hemoglobin, the globin contains two α-chains and two β-chains.
b) In fetal hemoglobin, there are two α chains and two γ-chains instead of β-chains.
FUNCTIONAL DIFFERENCES:_
a)Regarding functional point of view, fetal hemoglobin exhibits more affinity for oxygen than that of
adult hemoglobin.
b)And, the oxygenhemoglobin dissociation curve of fetal blood is shifted to
left
6. • ABNORMAL HEMOGLOBIN:-
• Abnormal types of hemoglobin or hemoglobin variants are the pathologic mutant forms of
hemoglobin.
• The production of These variants occurs due to especially structural changes in the polypeptide
chains caused by mutation in the genes of the globin chains.
• Most of the mutations do not result in any serious problem. Occasionally, few mutations lead to
some disorders.
•
• There are two types of abnormal hemoglobin:
• 1. Hemoglobinopathies
• 2. Hemoglobin in thalassemia and related disorders.
7. • 1. HEMOGLOBINOPATHIES
• Hemoglobinopathy is a genetic disorder happened by abnormal polypeptide chains of hemoglobin. Some of the
hemoglobinopathies are:
•
• I. Hemoglobin S
• It is observed in sickle cell anemia. In this, the α-chains are normal and β-chains are abnormal.
• ii. Hemoglobin C
• The β-chains are abnormal. It is seen in people with hemoglobin C disease, which is manifested by mild hemolytic anemia as
well as splenomegaly.
• iii. Hemoglobin E:
• Here also the β-chains show abnormality. It is observed in people with hemoglobin E disease which is also manifested by mild
hemolytic anemia and splenomegaly.
• iv. Hemoglobin M:
• a)It is the abnormal hemoglobin present in the form of methemoglobin.
• b) It happens because of mutation of genes of both in α and β chains, leading to abnormal replacement of amino acids.
• c)It is seen in babies affected by hemoglobin M disease or blue baby syndrome. It is an inherited disease, manifested by
characterized by methemoglobinemia
8. • BUFFER FUNCTION:-
• Hemoglobin behaves as a buffer and plays an important role in acidbase balance.
•
STRUCTURE OF HEMOGLOBIN
• Hemoglobin is a conjugated protein. It contains a protein combined with an ironcontaining pigment.
• The protein part is globin and the iron containing pigment is heme.
• Heme also forms a part of the structure of myoglobin (oxygen binding pigment in muscles) and neuroglobin (oxygen binding
pigment in brain)
• IRON:-
• Generally, it is seen in ferrous (Fe2+) form. It is in unstable or loose form.
• In some abnormal conditions, the iron is changed into ferric (Fe3+) state, which is a stable form.
•
• PORPHYRIN:-
• The pigment part of heme is ternmed as porphyrin. It is formed by four pyrrole rings (tetrapyrrole) termed as, I, II, III and IV.
• The pyrrole rings are bound to one another by methane (CH4 ) bridges. The iron is bound to ‘N’ of each pyrrole ring and ‘N’ of
globin molecule.
• GLOBIN:-
• Globin consists of four polypeptide chains. Among the four polypeptide chains, two are chains and two are α-chains
9. • TYPES OF NORMAL HEMOGLOBIB
• Hemoglobin is of two types:
• 1. Adult hemoglobin – HbA
• 2. Fetal hemoglobin – HbF
• Replacement of fetal hemoglobin by adult hemoglobin begins immediately after birth.
•
• SOURCES OF CABON MONOXIDE:-
• 1. Charcoal burning
• 2. Coal mines
• 3. Deep wells
• 4. Underground drainage system
• 5. Exhaust of gasoline engines
• 6. Gases from guns and other weapons
• 7. Heating system with poor or improper ventilation
• 8. Smoke from fire
• 9. Tobacco smoking
10. • SIGNS AND SYMPTOMS OF CARBON MONO OXIDE POISONING:-
•
• 1. While breathing air with less than 1% of CO, the Hb saturation is 15% to 20% and mild
symptoms like headache and nausea occur
•
• 2. While breathing air with more than 1% CO, the Hb saturation is 30% to 40%. It results in
severe symptoms such as:
• i. Convulsions
• ii. Cardio respiratory arrest
• iii. Unconsciousness and coma.
•
• When Hb saturation enhances above 50%, death occurs.
11. • METHMOGLOBIN:-
• Methemoglobin is the abnormal hemoglobin derivative formed if iron molecule of hemoglobin is
oxidized from normal ferrous state to ferric state. Methemoglobin
• is also termed as ferrihemoglobin.
• Normal methemoglobin level is 0.6% to 2.5% of total
• hemoglobin.
• Under normal circumstances also, body faces the threat of continuous production of
methemoglobin. But it is counteracted by erythrocyte protective system termed as nicotinamide
adenine dinucleotide (NADH) system, which operates with the help of two enzymes:
•
• 1. Diaphorase I (nicotinamide adenine dinucleotide phosphate [NADPH]dependent reductase):
Responsible for 95% of the action.
•
• Diaphorase II (NADPHdependent methemoglobin reductase): Responsible for 5% of the action.
• METHEMOGLOBINEMIA;_
• Methemoglobinemia is the disorder manifested by high level of methemoglobin in blood. It lresults
in tissue hypoxia, which causes cyanosis and other symptoms
12. • 2. HEMOGLOBIN IN THALASSEMIA AND RELATED DISORDERS:
•
• In thalassemia, different types of abnormal hemoglobins are observed. The polypeptide chains are
decreased, absent or abnormal.
• In α-thalassemia, the α-chains are decreased, absent or abnormal and in β-thalassemia, the β-
chains are decreased, absent or abnormal .
• Some of the abnormal hemoglobins found in thalassemia are hemoglobin G, H, I, Bart’s, Kenya,
Lepore and constant spring
13. • ABNORMAL HEMOGLOBIN DERIVATIVES
• ‘Hemoglobin derivatives’ refer to a blood test to identifyt and measure the percentage of abnormal hemoglobin derivatives.
• Hemoglobin is the only carrier particularly for transport of oxygen, without which tissue death happens within few minutes.
• When hemoglobin is altered, its oxygen carrying capacity is reduced leading to lack of oxygen. So, it is important to know about the causes and the effects of
abnormal hemoglobin derivatives.
• Abnormal hemoglobin derivatives are formed by carbon monoxide (CO) poisoning or due to some drugs like nitrites, nitrates and sulphanamides.
• ABNORMAL HEMOGLOBIN DERIVATIVES INCLUDE:-
•
• 1. Carboxyhemoglobin
• 2. Methemoglobin
• 3. Sulfhemoglobin.
• Normal percentage of hemoglobin derivatives in total hemoglobin:
• Carboxyhemoglobin : 3% to 5 %
• Methemoglobin : less than 3%
• Sulfhemoglobin : trace (undetectable).
• Abnormally high levels of hemoglobin derivates in blood lead to serious effects. These derivatives inhibit the transport of oxygen resulting in oxygen lack in tissues,
which may be fatal
14. • CARBOXY HEMOGLOBIN:-
• a)Carboxyhemoglobin or carbon monoxyhemoglobin is the abnormal hemoglobin derivative formed by the combination of carbon monoxide along with hemoglobin.
• b)Carbon monoxide is a colorless and odorless gas. Since hemoglobin has200 times more affinity for carbon monoxide than oxygen, it inhibits the transport of
oxygen leading to tissue hypoxia.
• c)Generally, 1% to 3% of hemoglobin is in the form of carboxyhemoglobin. 80 Section 2 t Blood and Body Fluids
• CAUSES OF METHEMOGLOBINEMIA:-
• Methemoglobinemia is influenced by variety of factors:
• 1. COMMON FACTORS OF DAILY LIFE:-
• i. Well water contaminated with nitrates and nitrites
• ii. Fires
• iii. Laundry ink
• iv. Match sticks and explosives
• v. Meat preservatives (which contain nitrates and
• nitrites)
• vi. Mothballs (naphthalene balls)
• vii. Room deodorizer propellants.
•
• 2. EXPOSURE TO INDUSTRIAL CHEMICALS NAMELY:-
• i. Aromatic amines
• ii. Fluorides
• iii. Irritant gases like nitrous oxide and nitrobenzene
• iv. Propylene glycol dinitrate
15. • 3.DRUGS;-
• i. Antibacterial drugs namely sulfonamides
• ii. Antimalarial drugsnamely chloroquine
• iii. Antiseptics
• iv. Inhalant in cyanide antidote kit
• v. Local anesthetics namely benzocaine.
•
• 4. HEREDITARY TRAIT:-:
• a)Because of deficiency of NADH-dependant reductase or presence of abnormal hemoglobin M.
• b)Hemoglobin M is common in babies influenced by blue baby syndrome (a pathological condition
in infants, manifested by bluish skin discoloration (cyanosis), caused by congenital heart
• defect)
16. • BLOOD LEVEL OF SULFEHEMOGLOBIN:-
• Generally, very negligible amount of sulfhemoglobin is observed in blood which is nondetectable.
But when its level rises above 10 gm/dL, cyanosis happens Normally, serious toxic effects are not
observed..
• SYNTHESIS OF HEMOGLOBIN-
• Synthesis of hemoglobin actually begins within proerythroblastic stage . Whatever it may be ,
hemoglobin appears in the intermediate normoblastic stage only.
b)Continuation of the production of hemoglobin happens until the stage of reticulocyte.
• c) Heme portion of hemoglobin is synthesized in mitochondria and the protein part, globin is
synthesized in ribosomes
17. • SYNTHESIS OF HEME:-
• Heme is synthesized from succinylCoA and the glycine. The sequence of events in synthesis of hemoglobin:
•
• 1. First step in heme synthesis happens in the mitochondrion. Two molecules of succinylCoA bind with two molecules of glycine and
condense to form δ-aminolevulinic acid (ALA) by ALA synthase.
•
• 2. ALA is transported to the cytoplasm. Two molecules of ALA combine to form porphobilinogen in the presence of ALA dehydratase.
•
• 3. Porphobilinogen is converted into uroporphobilinogen I by uroporphobilinogen I synthase.
•
• 4. Uroporphobilinogen I is converted into uropor phobilinogen III by porphobilinogen III cosynthase.
•
• 5. From uroporphobilinogen III, a ring structure termed as coproporphyrinogen III is formed by
• Particulary uroporphobilinogen decarboxylase.
•
• 6. Coproporphyrinogen III is transported back to the mitochondrion, where it is oxidized to form protoporphyrinogen IX by
coproporphyrinogen oxidase
•
• 7. Protoporphyrinogen IX is converted into protoporphyrin IX by protoporphyrinogen oxidase.
•
• 8. Protoporphyrin IX combines with iron to form heme especially in the presence of ferrochelatase
18. • FORMATION OF GLOBIN:-
• The production of Polypeptide chains of globin occurs in in the ribosomes. b)There
are four types of polypeptide chains such as, alpha, beta, gamma and delta chains.
• Each of these chains differs from others because of the amino acid sequence. The formatioon of
each globin molecule occurs by the combination of 2 pairs of chains and each chain I consists of
141 to 146 amino acids.
• Adult hemoglobin consists of two alpha chains and two beta chains. Fetal hemoglobin consists of
two alpha chains and two gamma chains
19.
20. • DESTRUCTION OF HEMOGLOBIN:-
• a)After the lifespan of 120 days, the RBC is demolished especially in the reticuloendothelial
system, particularly in spleen and the hemoglobin is released into plasma.
• b)Soon, the hemoglobin is deteriorated in the reticuloendothelial cells and divide into globin and
heme.
• c)Globin is utilized for the resynthesis of hemoglobin. Heme is degraded into iron and porphyrin.
• d) Iron is stored in the body as ferritin and hemosiderin, which are reutilized for the synthesis of new
hemoglobin.
• e)Porphyrin is changed into a green pigment called biliverdin. In human being, most of the
biliverdin is changed into a yellow pigment called bilirubin. Bilirubin and biliverdin are together
called the bile pigments
21. • References
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Publishing; Treasure Island (FL): Nov 23, 2022. Oxygen
Saturation. [PubMed]2. Chiabrando D, Mercurio S,
Tolosano E. Heme and erythropoieis: more than a
structural role. Haematologica. 2014 Jun;99(6):973-83.
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AM. StatPearls [Internet]. StatPearls Publishing;
Treasure Island (FL): Sep 4, 2023. Alpha Thalassemia.
[PubMed]4. Edel Y, Mamet R. Porphyria: What Is It
and Who Should Be Evaluated? Rambam Maimonides Med J.
2018 Apr 19;9(2) [PMC free article] [PubMed]5.
Farashi S, Harteveld CL. Molecular basis of α-
thalassemia. Blood Cells Mol Dis. 2018 May;70:43-53.
[PubMed]6. Forget BG, Bunn HF. Classification of
the disorders of hemoglobin. Cold Spring Harb Perspect
Med. 2013 Feb 01;3(2):a011684. [PMC free article]
[PubMed]7. Needs T, Gonzalez-Mosquera LF, Lynch DT.
StatPearls [Internet]. StatPearls Publishing; Treasure
Island (FL): May 1, 2023. Beta Thalassemia. [PubMed]8.