Protien Metabolism
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The structure of a protein determines its function. For enzymes, the binding site or active site allows substrates to bind via lock-and-key or induced fit mechanisms. Myoglobin and hemoglobin both contain heme groups to bind oxygen, but differ in structure - myoglobin is spherical while hemoglobin is a tetramer. This allows hemoglobin to exhibit cooperative binding and transport oxygen more efficiently than myoglobin via conformational changes.
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Protien Metabolism
The structure of a protein determines its function. For enzymes, the binding site or active site allows substrates to bind via lock-and-key or induced fit mechanisms. Myoglobin and hemoglobin both contain heme groups to bind oxygen, but differ in structure - myoglobin is spherical while hemoglobin is a tetramer. This allows hemoglobin to exhibit cooperative binding and transport oxygen more efficiently than myoglobin via conformational changes.
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myoglobin
Myoglobin is a protein found in muscle tissue that binds oxygen. It was the first protein whose three-dimensional structure was determined using X-ray crystallography in the 1950s-60s. Myoglobin facilitates oxygen transport within muscles through reversible binding of oxygen to an iron-containing heme group. It stores oxygen to help meet rapid energy demands in muscle cells and prevents accumulation of toxic nitric oxide.
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Oxygen Binding by Myoglobin and Hemoglobin
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1. The document discusses heme proteins such as hemoglobin and myoglobin. Hemoglobin transports oxygen in red blood cells, while myoglobin stores oxygen in muscle cells.
2. Both hemoglobin and myoglobin contain a heme group which binds oxygen. In hemoglobin, the binding of oxygen to one heme group facilitates binding to the other heme groups, known as cooperativity.
3. Environmental factors like pH and carbon dioxide concentration affect oxygen binding and release from hemoglobin, known as the Bohr effect. A lower pH or higher carbon dioxide leads to oxygen being more readily released from hemoglobin.
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Protien Metabolism
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2. Both hemoglobin and myoglobin contain a heme group which binds oxygen. In hemoglobin, the binding of oxygen to one heme group facilitates binding to the other heme groups, known as cooperativity.
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Hemoglobin is a protein in red blood cells that transports oxygen and carbon dioxide throughout the body. There are three main types of hemoglobin in humans: hemoglobin A, hemoglobin F, and hemoglobin A2. Hemoglobin has a structure of four subunits, each containing a globular protein chain and a heme group with iron. The structure allows hemoglobin to reversibly bind oxygen in the lungs and release it in tissues through a conformational change between tense and relaxed states. Diseases can arise from structural variants that decrease stability or from disorders in globin chain synthesis.
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This document provides an introduction to hemoglobin and myoglobin, including their structures, functions, and a comparison between the two. Hemoglobin is an oxygen-transport protein found in red blood cells that binds to oxygen in the lungs and delivers it to tissues throughout the body. Myoglobin is an oxygen-storage protein found in muscle tissue that stores oxygen for use within muscles. Both proteins use a heme group containing iron to reversibly bind oxygen, but hemoglobin is a heterotetramer made of two alpha and two beta chains, while myoglobin is a monomer. The document also discusses cooperative binding in hemoglobin and allosteric regulation.
Metalloporphyrins with special reference to Iron porphyrins ( Haemoglobin and...
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❑ These porphines act as tetradentate ligands with four
nitrogen donor sites.
Two of these are tertiary nitrogen donor positions which can form
coordinate bonds by donating a pair of electrons each to the metal
ion.
❑ The other two are secondary nitrogen donor positions. each of
which lose a proton in forming a coordinate bond with a metal
ion.
❑ Thus, a porphin ring acts as a tetradentate dinegative ligand (or
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❑ Dipositive cations such as Mg2+ Fe2+ or Ni2+ are capable of
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❑ Four pyrrole rings of porphin carrying substituents other than hydrogen
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This document provides information on hemoglobin, including its structure, function, and role in oxygen transport. Key points include:
- Hemoglobin is an iron-containing protein in red blood cells that carries oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs.
- It consists of a protein component called globin and a non-protein component called heme, which contains iron.
- Hemoglobin has a tetrameric structure composed of two alpha and two beta subunits, each containing a heme group that reversibly binds oxygen.
- The binding of oxygen to one subunit influences the binding of oxygen to other subunits, allowing hemoglobin to load and unload oxygen cooperatively in response to changes in oxygen
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INTRODUCTION
DISCOVREY OF MYOGLOBIN STRUCTURE
STRUCTURE OF MYOGLOBIN
APOMYOGLOBIN
MECHANISM-
BINDING OF OXYGEN TO MYGLOBIN
DISASSOCIATION OF OXYGEN FOROM MYOGLOBIN
IMPORTANT FEATURES OF MYOGLOBIN
BIOLOGICAL SIGNIFICANCES OF MYOGLOBIN
CONCLUSION
REFERENCES
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Myoglobin transports oxygen from capillaries to mitochondria in muscle tissue. It contains a heme group that can bind one oxygen molecule to form oxymyoglobin. Oxygen binds to the iron atom of the heme group through hydrophobic and histidine interactions. Myoglobin binds oxygen noncooperatively, as shown by its hyperbolic titration curve, and has a higher affinity for oxygen than hemoglobin due to its lower p50 value.
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Hemoglobin and myoglobin are heme proteins that bind oxygen. Hemoglobin transports oxygen from the lungs to tissues, while myoglobin stores and facilitates oxygen diffusion in muscle tissue. Hemoglobin binds oxygen cooperatively through interactions between its subunits, allowing it to fully saturate with oxygen in the lungs but release 40% of its oxygen at lower oxygen tensions in the veins. Myoglobin binds oxygen noncooperatively. The binding affinity of both proteins is decreased by factors like protons (Bohr effect), carbon dioxide, and BPG, enhancing oxygen release to tissues. These properties allow hemoglobin and myoglobin to optimize oxygen delivery and storage in mammals.
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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.
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The document summarizes the structure and function of hemoglobin. Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It is composed of heme and globin proteins. Heme contains iron and is produced in mitochondria, while globin chains are produced by ribosomes and combine with heme to form hemoglobin. The main types of hemoglobin in humans are fetal hemoglobin during development and adult hemoglobin after birth. Hemoglobin transports oxygen via an oxygen-binding reaction that allows it to efficiently deliver oxygen to tissues and receive carbon dioxide.
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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.
Hemoglobin
Hemoglobin is the protein in red blood cells that carries oxygen. It is made up of heme and globin subunits produced in different parts of the cell. Hemoglobin binds to oxygen molecules in the lungs and transports oxygen to tissues throughout the body, where it releases the oxygen to tissues and picks up carbon dioxide to carry back to the lungs. Each red blood cell contains over 640 million hemoglobin molecules to facilitate this gas exchange process.
Hemoglobin and _myoglobin
Globular proteins like hemoglobin and myoglobin have complex tertiary and sometimes quaternary structures that allow them to perform important biological functions. Hemoglobin is a transport protein that carries oxygen in the bloodstream through a heme group and heterotetrameric structure. Myoglobin is a storage protein found in muscle tissue that stores oxygen through a monomeric structure. Both proteins bind oxygen through histidine residues interacting with iron in their heme groups, but hemoglobin has higher cooperativity and can bind four oxygen molecules at once. Proteins are essential for many biological processes like structure, movement, transport, immune response and more.
Hemoglobin
Haemoglobin is the protein in red blood cells that transports oxygen and carbon dioxide throughout the body. It is composed of four globin protein subunits, each containing an iron-containing heme group. Haemoglobin's ability to bind and release oxygen and carbon dioxide allows it to deliver oxygen from the lungs to tissues and remove carbon dioxide from tissues back to the lungs. Several factors regulate haemoglobin's affinity for oxygen, including partial pressures of oxygen and carbon dioxide, pH, and levels of 2,3-bisphosphoglycerate in the blood. This complex regulation allows haemoglobin to efficiently load and unload gases where they are needed.
Biochemistry of blood, respiratory function of erythrocytes
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This document summarizes the key functions and processes related to blood, red blood cells, hemoglobin, oxygen transport and carbon dioxide transport. It discusses how hemoglobin binds and transports oxygen and carbon dioxide in the body, and how pH, carbon dioxide levels and 2,3-BPG affect hemoglobin's affinity for oxygen. It also summarizes sickle cell anemia and thalassemias.What's hot (20)
Metalloporphyrins with special reference to Iron porphyrins ( Haemoglobin and...
Metalloporphyrins with special reference to Iron porphyrins ( Haemoglobin and...
Role of hemoglobin and myoglobin in biological systems
Role of hemoglobin and myoglobin in biological systems
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Role of co-ordination chemistry in myoglobin chemistry Myoglobin
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Structure Of Hemoglobin and Difference between Fetal and Adult Hemoglobin.
Biochemistry of blood, respiratory function of erythrocytes
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The document summarizes protein synthesis through the central dogma of genetics. It discusses how DNA is transcribed into mRNA which is then translated into proteins using tRNA and ribosomes. The main stages of translation - initiation, elongation, and termination - are also outlined. Finally, the genetic code table is shown, which demonstrates how mRNA codons correspond to specific amino acids.
Protein metabolism
1. Protein metabolism involves the breakdown of amino acids into ammonia and carbon skeletons, and the reuse of these components for new protein synthesis or energy production. Amino acids undergo transamination, deamination, and are metabolized through the urea cycle to dispose of ammonia.
2. The urea cycle is a series of chemical reactions that converts ammonia into urea for excretion. It occurs primarily in the liver and involves five enzymatic steps to incorporate ammonia and carbon into the relatively non-toxic urea molecule.
3. Defects in protein metabolism can cause inborn errors such as phenylketonuria, maple syrup urine disease, and defects in the urea cycle, which
Protein metabolism
Protein metabolism involves the breakdown of proteins into amino acids and their use and degradation throughout the body. Amino acids from food sources are broken down through digestion and absorbed. They are used for protein synthesis, forming hormones and other compounds, and undergo constant breakdown and renewal to replenish amino acid reserves. Excess amino acids have their nitrogen removed through transamination or oxidative deamination, producing ammonia. The liver plays a key role in nitrogen excretion by converting toxic ammonia into less toxic urea via the urea cycle, which is then excreted in urine.
Protein and-peptide-drug-delivery-systems
The document discusses protein and peptide drug delivery systems. It begins by defining proteins and peptides, noting that proteins are molecules composed of over 50 amino acids, while peptides are molecules composed of less than 50 amino acids. It then discusses how scientific advances in molecular and cell biology have led to the development of recombinant DNA and hybridoma technology to produce protein products. The document provides examples of marketed protein and peptide drugs and discusses challenges with delivering these drugs orally due to their large molecular size and susceptibility to enzymatic degradation. It explores approaches to protein and peptide delivery including non-parenteral systemic delivery methods and various considerations for developing delivery systems for these pharmaceuticals.
Protein and peptide drug delivery system
Protein and Peptide drug delivery system are the Novel drug Delivery System. Proteins and peptides are the most abundant components of biological cells. They exist functioning such as
enzymes, hormones, structural element and immunoglobulin. The distinction between peptides and proteins is having a peptide contains less than 20 amino acids, having a molecular weight less, while a protein possesses 50 or more amino acids and its molecular weight lies above this value. The most of pharmaceutical proteins and peptides are absorbed IM, IV and Subcutaneous route of Absorption, but the oral route is more convenient for absorption of protein as compared to other. Various problems associated with administration of protein and peptide drugs are needed to overcome by different pharmaceutical approaches. Several approaches available for
maximizing pharmacokinetic and pharmacodynamics properties are chemical modification,
formulation vehicles, mucoadhesive polymeric system, use of enzyme inhibitors, absorption
enhancers, penetration enhancers etc.
Biochemistry ii protein (metabolism of amino acids) (new edition)
This document discusses the metabolism of amino acids. It begins with an introduction and overview of amino acid classification, definitions of terms like nitrogen balance and biological value, and the digestion and absorption of proteins. It then covers the metabolic fates of amino acids, including removal of ammonia via deamination, transamination, and transdeamination. The carbon skeletons of amino acids can be used for biosynthesis, the synthesis of non-protein nitrogen compounds, or energy production. Ammonia is further metabolized. Overall, the document provides a comprehensive overview of the key processes in amino acid metabolism.
Protein and peptide delivery system
This slide show is created for the purpose of helping pharma people involved in research in drug delivery methods.
Collagen! - The connective Tissue Protein
This was a seminar I had done for my Biochemistry class while studying naturopathy and yoga -BNYS (1st Year). enjoy.
Pharmacology of Peptides and Proteins
This document provides an overview of pharmacology of proteins and peptides. It discusses the historical perspective of peptide research beginning in the 1930s. Key developments include the elucidation of the structures of oxytocin and vasopressin by Dr. Vincent du Vigneaud in the 1950s. The document compares neuropeptides to conventional neurotransmitters and describes the biosynthesis and regulation of proteins. It also covers topics such as proteins and peptides as drugs, peptide agonists and antagonists, and techniques for identifying, isolating, and characterizing peptides. The future potential of designer proteins is also mentioned.
protein and peptide drug delivery system
This document discusses protein and peptide drug delivery systems. It begins by defining proteins and peptides, and their importance in biological functions and pharmaceuticals. It then covers the classification and structures of proteins. Various routes of administration for protein and peptide drugs are examined, including parenteral routes like intravenous, intramuscular, and subcutaneous. Specific drug delivery systems like polymer-based, liposome-based, and hydrogel-based systems are outlined. Both implantable and mechanical pumps are mentioned for prolonged parenteral delivery. Non-parenteral routes such as oral, nasal, pulmonary and transdermal are also reviewed.
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
Amino Acids metabolism
This document discusses protein metabolism and the metabolism of amino acids. It notes that proteins are the most abundant organic compounds in the body, making up 10-12kg of dry weight, and perform many structural and functional roles. Amino acids are the building blocks of proteins and there are 20 naturally occurring amino acids, with 10 being non-essential and needing to be synthesized by the body. The amino acid pool is maintained through intake from dietary proteins and synthesis of non-essential amino acids, and is utilized for protein synthesis and other metabolic processes. Protein metabolism involves the constant breakdown and resynthesis of body proteins.
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Biochemistry ii protein (metabolism of amino acids) (new edition)
Biochemistry ii protein (metabolism of amino acids) (new edition)
Similar to Protien Metabolism
Protein ligand interaction
This is based on protein-ligand interaction physical method, which gives us knowledge about how our body protein interacts with other molecule and protein function.
Protein ligand interaction by KK Sahu sir
The document discusses protein-ligand interactions, providing examples of hemoglobin and antibodies. It explains that proteins interact specifically with ligands through binding sites, and this interaction is important for functions like oxygen transport and immune response. Hemoglobin transports oxygen through a cooperative binding process where the binding of oxygen to one subunit affects the affinity of nearby subunits. Antibodies also bind specifically to antigens through complementary interaction, which is vital for the immune system. The reversible and specific nature of protein-ligand binding allows for important biological processes and applications.
slides conjugate proteins (1).pptx
The document discusses the molecular basis of hemoglobin and hemoglobinopathies. It describes the structures and functions of myoglobin and hemoglobin, comparing their oxygen binding properties. Hemoglobin has a sigmoidal oxygen binding curve due to its allosteric properties arising from quaternary structure. Effectors like CO2, H+, chloride ions, and 2,3-BPG regulate hemoglobin's affinity for oxygen. The molecular basis of sickle cell anemia is explained, with the point mutation causing hemoglobin tetramers to aggregate and deform red blood cells, clogging capillaries. ELISA principles and importance for serodiagnosis of infectious diseases is briefly outlined.
Protein Function - General Biology 2 Lesson
Globular proteins function through reversible ligand binding. This chapter examines oxygen transport by hemoglobin and myoglobin, antibody-antigen interactions, and muscle contraction. Key concepts include cooperative binding in hemoglobin, which increases oxygen affinity in the lungs and decreases it in tissues, and the induced fit model where ligand binding causes conformational changes for functions like oxygen transport and muscle movement.
Haemoglobin
Hemoglobin 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 globular tetrameric protein composed of two alpha and two beta chains, with each chain containing a heme group that binds to oxygen. Hemoglobin undergoes a conformational change upon oxygen binding that makes the remaining binding sites have a higher affinity for oxygen in a cooperative binding process essential for oxygen transport.
HB.pdf
Hemoglobin is a conjugated protein found in red blood cells that carries oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs. It is composed of globin and heme. Globin contains four polypeptide chains (two alpha and two beta or gamma or delta chains) and four heme groups. Heme contains iron that reversibly binds oxygen. Hemoglobin binding of oxygen is cooperative, allowing for efficient oxygen delivery to tissues. Its affinity for oxygen decreases in tissues due to Bohr and BPG effects, promoting oxygen release to tissues.
Hemoglobin and myoglobin are two important proteins involved in the transport...
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.
Haemoglobin and Gas Transport.pptx
This document discusses the structure and function of haemoglobin and the transport of gases in the blood. It provides a history of discoveries about haemoglobin dating back to the 17th century. Key points covered include the tetrameric structure of haemoglobin, with each subunit binding one heme group and iron atom. Haemoglobin is able to efficiently transport oxygen and carbon dioxide via changes in its quaternary structure and binding of effectors like hydrogen ions, carbon dioxide and 2,3-BPG. The sigmoidal oxygen dissociation curve illustrates haemoglobin's ability to load and unload oxygen in the lungs and tissues respectively. Factors like pH, temperature and organic phosphates influence the curve.
GLOBULAR PROTEINS
This document provides an overview of globular proteins, with a focus on hemoglobin and myoglobin. It discusses the following key points:
- Globular proteins have hydrophilic amino acids on the outside and hydrophobic amino acids on the inside, allowing them to be soluble in water. Hemoglobin and myoglobin are important globular proteins.
- Hemoglobin transports oxygen in red blood cells, while myoglobin stores and transports oxygen in muscle cells. Both contain a heme group that reversibly binds oxygen.
- The structures of myoglobin and each subunit of hemoglobin involve alpha helices that form a pocket holding the heme group. Histidine residues help bind the heme iron and oxygen.
- Hemoglobin
Globular proteins
This ppt is free to use and learn. I have made it for seeking students. It has in it what I have written about globular proteins.
Hemoglobin and myoglobin
Hemoglobin and myoglobin are metalloproteins that carry oxygen in organisms. Hemoglobin transports oxygen from the lungs to tissues via the bloodstream. It contains four subunits, each with an iron-containing heme group that reversibly binds oxygen. Myoglobin stores oxygen in muscle tissues. It contains a single polypeptide chain with a heme group. Both proteins release oxygen in tissues through cooperativity and the Bohr effect, which decreases their oxygen affinity under acidic conditions produced by cellular respiration. Diseases like sickle cell anemia arise from mutations altering hemoglobin structure and function.
protein ligend interaction by kk sahu
Introduction
Common terms used
Protein ligand interaction
1)in oxygen binding protein
Heme
Structure of hemoglobin
Ligand binding effected by protein structure
Oxygenation &deoxygenation
Cooperative binding of oxygen
Models for cooperative binding
Hb also transports H+&co2
2)complementary interaction immune system &immunoglobulin
Introduction
Structure of antibodies
Binding of antigen to antibody
Applications
Conclusion
Reference
Porphyrins, haemoglobin and bilirubin
Porphyrins are organic compounds containing four pyrrole rings linked together with methenyl bridges. Biologically important porphyrins are usually conjugated with proteins. Important porphyrin-containing compounds include hemoglobin, myoglobin, cytochromes, catalase, and peroxidase. Hemoglobin is a conjugated protein made of four subunits, each containing a heme group with an iron ion. Hemoglobin can reversibly bind oxygen and transport it throughout the body. Porphyrin synthesis begins with the condensation of succinyl-CoA and glycine, and ultimately results in the formation of heme, which is critical for the function of various heme proteins.
lecture 1.pdfrgzdfghzdfhgzdfhfdhdzhzdhdhdhd
Gas exchange occurs in the alveoli of the lungs where oxygen diffuses from the inhaled air into the blood and carbon dioxide diffuses out of the blood and into the exhaled air. Hemoglobin is responsible for carrying oxygen in the blood from the lungs to tissues and carrying carbon dioxide back to the lungs from tissues. Hemoglobin has a higher affinity for oxygen when oxygen levels are high, like in the lungs, and a lower affinity when oxygen levels are low, like in tissues, through a cooperative binding mechanism that allows for efficient oxygen delivery throughout the body. Myoglobin stores and facilitates oxygen transport within muscle cells.
Hemoglobin structure
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.
4.Hemoglobin Type of O2 carriers.pdf
- Iron is an essential bioelement that plays a vital role in electron transfer processes in the body. It is present in heme proteins like hemoglobin and myoglobin.
- Hemoglobin transports oxygen from the lungs to tissues via red blood cells. It is a tetrameric protein with four heme groups that can bind oxygen cooperatively. Myoglobin stores and supplies oxygen to muscles. It is monomeric with one heme group.
- Both proteins contain a heme prosthetic group consisting of an iron ion bound to a porphyrin ring. The iron can reversibly bind oxygen. Hemoglobin and myoglobin facilitate oxygen transport and metabolism in vertebrates through these iron-oxygen interactions.
HAEMOGLOBIN PPT 1.ppt
- Hemoglobin (Hb) is an oxygen-transport protein found in red blood cells. It has a tetrameric structure composed of two alpha and two beta subunits, each containing an iron-containing heme group that reversibly binds oxygen.
- Hb binds oxygen cooperatively, meaning that the binding of oxygen to one subunit increases the affinity of the other subunits for oxygen. This allows for efficient oxygen uptake in the lungs and release in tissues.
- Factors like pH, carbon dioxide levels, and 2,3-bisphosphoglycerate regulate Hb's affinity for oxygen and allow for oxygen delivery to tissues where it is needed. Sickle cell anemia results from a mutation that causes Hb to polymer
Haemoglobin
Haemoglobin is an essential component of blood. It contains iron and protein and its deficiency can cause anaemia and can even be fatalic. This ppt is all about important aspects of Haemoglobin , its history,its pH dependance inside the body, sickle cell disease etc.
Hemoglobin structure and function.pptx
The document provides an overview of hemoglobin structure and function including:
- Hemoglobin transports oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs.
- It is composed of heme and globin proteins. Heme contains iron that reversibly binds oxygen.
- Factors like pH, carbon dioxide levels, and 2,3-BPG affect oxygen binding affinity and allow delivery of oxygen to tissues.
- Abnormal hemoglobins cannot transport oxygen due to structural defects.
Transport of o2 and co2 between respiratory surface
This document summarizes oxygen transport in blood and the factors that influence oxygen binding to hemoglobin. It discusses how hemoglobin transports oxygen by reversibly binding to it, and how oxygen dissociation curves describe this relationship. The curves are sigmoid for vertebrate hemoglobin and hyperbolic for other respiratory pigments. Factors like pH, temperature, CO2 levels, and organic phosphates influence the oxygen affinity by inducing conformational changes in hemoglobin. Together, these mechanisms facilitate oxygen loading in the lungs and unloading in tissues to meet metabolic demand.
Similar to Protien Metabolism (20)
Hemoglobin and myoglobin are two important proteins involved in the transport...
Hemoglobin and myoglobin are two important proteins involved in the transport...
Transport of o2 and co2 between respiratory surface
Transport of o2 and co2 between respiratory surface
More from raj kumar
The umbilical cord
The umbilical cord connects the fetus to the placenta and measures approximately 50 cm in length and 2 cm in diameter at term. It contains one vein that carries oxygenated blood to the fetus and two arteries that carry deoxygenated blood away. The cord inserts into the placenta near its center in most cases. Abnormalities can include abnormal insertion points, short or long length, knots, torsion, hematoma, or having a single umbilical artery instead of two.
The placenta
The placenta develops from fetal and maternal tissues to function as the respiratory, nutritive, excretory, barrier and endocrine organ of pregnancy. It transfers oxygen, nutrients and waste between the mother and fetus. The placenta can develop abnormalities in its shape, size, position or adhesion to the uterine wall which may cause complications like preterm birth or hemorrhage. Placental lesions like infarcts may also occur due to conditions like hypertension.
The foetal membranes
The document discusses the fetal membranes, which include the chorion and amnion. The chorion is the outer membrane that is attached to the placenta and uterine wall. The amnion lines the chorion and encloses the fetus and amniotic fluid. The amniotic fluid provides protection and nutrition for the fetus, and aids in temperature regulation and movement. It is composed primarily of water, carbohydrates, proteins and minerals. The amniotic fluid circulates continuously, with production from the fetal membranes, fetal urine and transudation from maternal and fetal blood.
Physiology of reproduction
The document summarizes the key stages in human reproduction from fertilization through early pregnancy development. It describes how sperm mature and are capacitated in the female reproductive tract. Upon ovulation, sperm meet and fertilize the ovum in the fallopian tubes. The zygote then undergoes cell division and develops into a blastocyst that implants in the uterus. The trophoblast cells of the blastocyst invade the uterine lining and develop into a placenta to exchange nutrients and waste with the mother's blood. Major developmental milestones in early pregnancy include chorion, amnion and decidua formation.
Minor complaints during pregnancy
The document discusses several minor complaints that may occur during pregnancy, including gingivitis, ptyalism, heartburn, constipation, hemorrhoids, varicosities, dyspnea, urinary symptoms, leucorrhea, leg cramps, paraethesia, and backache. For each complaint, the causes and recommended treatments are provided.
Diagnosis of pregnancy
This document discusses the diagnosis of pregnancy over three trimesters. In the first trimester, common symptoms include missed periods, morning sickness, frequent urination, and breast changes. Signs include enlarged, soft breasts and uterus, and a softer, purplish cervix. Pregnancy tests detect human chorionic gonadotropin in urine or blood. Ultrasounds can visualize the gestational sac after 4-5 weeks. In the second trimester, symptoms decrease while the abdomen enlarges and fetal movement is felt. Signs include skin changes and palpable fetal parts. The third trimester confirms pregnancy through palpation of fetal parts and auscultation of the fetal heart.
Antenatal care
Antenatal care involves regular checkups during pregnancy to monitor the health of the mother and baby. Checkups include exams, tests, and education on nutrition, exercise, hygiene, warning signs and avoiding risks. The goals are to prevent or treat complications, detect issues, and ensure healthy development. Women receive more frequent exams as their due date approaches, and are instructed on a nutritious diet, moderate exercise, adequate rest, hygienic practices, and when to seek medical help if problems arise.
Postpartum mood disorders
The document discusses postpartum mood disorders, including prevalence, risk factors, screening tools, diagnosis, and treatment options. It notes that postpartum mood disorders range from mild and temporary postpartum blues to more severe postpartum depression and postpartum psychosis. Screening tools like the Edinburgh Postnatal Depression Scale can help identify at-risk women. Treatment involves psychosocial therapies and may include antidepressant medication depending on severity. A multidisciplinary approach is important to address biological, psychological and social factors.
Normal and abnormal puerperium
Uterine fibroids are benign smooth muscle tumors that develop in the uterus. They are the most common solid pelvic tumors, affecting 20-25% of women during their reproductive years. Fibroids can vary in size and location, and may cause heavy menstrual bleeding, pelvic pressure or pain. Treatment options include observation, medical therapy to reduce estrogen levels, or surgical removal of fibroids.
Version
Version refers to changing the fetal lie or position in the uterus. There are three main types: external cephalic version, internal podalic version, and bipolar podalic version. External cephalic version involves manipulating the fetus externally to convert a breech presentation to head-first. Internal podalic version is performed under anesthesia when the cervix is fully dilated to grasp the fetus's feet and convert a transverse lie to breech. Bipolar podalic version uses both internal and external manipulation through a partially dilated cervix for special circumstances. Complications can include fetal distress, premature separation of the placenta, and maternal hemorrhage.
Vacuum extraction (ventouse)
Vacuum extraction is a method to assist in childbirth using suction from a cup placed on the baby's head to help with traction during contractions. There are different types of cups including metal, soft, and bird's cups. Vacuum extraction is indicated when forceps cannot be used and has advantages over forceps like less need for anesthesia and less compression force applied. Complications can include maternal lacerations and cervical injuries or fetal issues like cephalhematomas and scalp lacerations.
Symphysiotomy
Symphysiotomy is a surgical procedure that divides the symphysis pubis bone to widen the pelvis during childbirth. It is indicated when cephalopelvic disproportion makes vaginal delivery difficult or dangerous but cesarean section is not available or advised. The procedure involves making a small incision above the pubic bone and gradually separating the joint using a scalpel. Complications can include bleeding, injury to nearby organs, infection, and long-term issues like incontinence or an unstable pelvis.
Forceps delivery
This document discusses obstetric forceps, which are metal instruments used to extract a baby's head during delivery. It describes different types of forceps and their proper application techniques. Forceps are indicated for prolonged second stage of labor, maternal distress, or fetal distress. Correct application involves inserting one blade along each side of the baby's head. Potential complications include laceration, hemorrhage, nerve injury, or problems for the baby such as skull fractures. Failure to deliver with forceps may require removal and assessment to determine if cesarean section is needed.
Episiotomy
This document discusses episiotomy, which is an incision made in the perineum during childbirth to widen the vaginal opening. It can help prevent tearing and complications. The two main types are median and mediolateral episiotomies. Median episiotomies involve a midline incision while mediolateral incisions extend laterally towards the ischial tuberosity. Episiotomies are usually performed when the vaginal opening is distended during crowning to prevent stretching injuries. They are sutured closed after delivery.
Caesarean section
The document discusses Caesarean section, including indications, types, procedure, complications, and mode of delivery in subsequent pregnancies. A Caesarean section is a surgical procedure to deliver one or more babies through incisions in the abdomen and uterus. The rate of Caesarean sections has increased from 5% in 1970 to 25% in 1990 due to factors such as abandoning difficult procedures in favor of C-sections and increased use for breech births. Complications can include hemorrhage, infections, and injuries to the mother or baby.
Normal labour
Normal labour involves the spontaneous expulsion of a single, mature fetus through the birth canal within 3-18 hours without complications. It occurs when hormonal and mechanical factors cause the cervix to efface and dilate in stages from 3cm to full 10cm dilation. Labour proceeds through four stages: 1) cervical dilation, 2) expulsion of the fetus, 3) expulsion of the placenta, and 4) recovery. The fetus descends through the birth canal with increased flexion to facilitate delivery of the head.
Anatomy of the foetal skull
The fetal skull consists of three parts: the vault, face, and base. The vault is made up of the frontal, parietal, and occipital bones which are separated by sutures. The face extends from the chin to the nose. Fontanelles are soft spots located where sutures meet which are important for assessing fetal position and flexion. The skull has various longitudinal and transverse diameters used to determine which will engage and pass through the birth canal during delivery.
Anatomy of the female pelvis
The female pelvis is divided into the false pelvis and true pelvis. The true pelvis is further divided into the pelvic inlet, cavity, and outlet. The document describes the boundaries and diameters of each region including the anatomical transverse diameter of 13cm at the inlet. It also discusses the pelvic planes and axes, and the Caldwell-Moloy classification of pelvic types including the gynaecoid, anthropoid, android, and platypelloid pelvis.
Active management of normal labour
This document outlines the active management of normal labour in 4 stages: antenatal preparation, first stage (history, exam, procedures), second stage (delivery of baby), third stage (delivery of placenta), and fourth stage (postpartum care of mother and baby). The goal is a healthy delivery with minimal effects. Key procedures include monitoring contractions/fetal heart with a partogram, positioning, nutrition, analgesia, perineal support, and immediate newborn care.
Thyrotoxicosis in pregnancy
Thyrotoxicosis in pregnancy can cause complications like abortion and preterm labour. Clinical features include weight loss, heat intolerance, tremors, and fast heart rate. It is treated with antithyroid drugs like propylthiouracil or carbimazole. Epilepsy in pregnancy commonly presents as grand mal seizures, which are treated with phenobarbitone or phenytoin along with folic acid. Rhesus isoimmunization occurs when an Rh-negative mother develops antibodies against Rh-positive blood from her baby. It can be prevented by giving the mother anti-D immunoglobulin after delivery or pregnancy events involving blood transfer from baby to mother. Affected babies may require monitoring, phot
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Protien Metabolism
- 1. Protein Function Structure will determine the function of the protein www.freelivedoctor.com
- 16. Hemoglobin Binding Curve www.freelivedoctor.com