The document provides information on gel electrophoresis techniques. It discusses different types of gels like agarose, polyacrylamide, and starch that can be used for electrophoresis. Agarose gel is commonly used to separate macromolecules like nucleic acids and proteins due to its large pore size. Polyacrylamide gel is used to separate smaller molecules and provides better resolution than agarose. SDS-PAGE allows separation based on molecular weight by making all proteins negatively charged. The document outlines the procedures for agarose and polyacrylamide gel electrophoresis and their applications in analyzing proteins and nucleic acids.
Sepration of molecules on the basis of applied Electric Field
Categorized into 1) Zone Electrophoresis 2) Moving Boundary Electrophoresis
We can seprate macromolecules (DNA , RNA, PROTEINS )on the basis of their charge, size shape & molecular weight
Sepration of molecules on the basis of applied Electric Field
Categorized into 1) Zone Electrophoresis 2) Moving Boundary Electrophoresis
We can seprate macromolecules (DNA , RNA, PROTEINS )on the basis of their charge, size shape & molecular weight
The technique of paper electrophoresis is simple and inexpensive and requires only micro quantities of plasma for separation.
The support medium is a filter paper
The electrophoresis apparatus in its simplest form consists of two troughs to contain buffer solution, through which electric current is passed.
Frequently used in isolating proteins, amino acids and oligopeptides.
In this slide contains types, working principle, factors affecting, advantage and disadvantage of paper electrophoresis.
Presented by: G.Sai Swetha. (Department of pharmacology),
RIPER, anantapur.
It is a subtype of the gel electrophoresis whereby the normal gel is replaced with polyacrylamide gels used as support media.
Gels are made by free radical-induced polymerization of acrylamide and N,N’-Methylenebisacrylamide.
It is the most widely used technique of electrophoresis.
Isoelectric focusing electrophoresis- Principle , procedure and applicationsJaskiranKaur72
IEF separates amphoteric compounds, such as proteins, with increased resolution in a medium possessing a stable pH gradient. The protein becomes “focused” at a point on the gel as it migrates to a zone where the pH of the gel matches the protein's pI. At this point, the charge of the protein becomes zero and its migration ceases.
ION EXCHANGE CHROMATOGRAPHY
ByM.Vharshini
B.Sc. Bio Medical Science
Sri Ramachandra University
ION EXCHANGE CHROMATOGRAPHY
Ion-exchange chromatography is a process that allows the separation of ions and polar molecules based on their affinity to the ion exchanger.
It can be used for almost any kind of charged molecule including large proteins, small nucleotides and amino acids.
Cations or Anions can be separated using this method.
PRINCIPLE
It is based on the reversible electrostatic interaction of ions with the separation matrix (i.e.)
The separation occurs by reversible exchange of ions between the ions present in the solution and those present in the ion exchange resin.
CLASSIFICATION OF RESINS
According to the chemical nature they classified as-
1. Strong cation exchange resin
2. Weak cation exchange resin
3. Strong anion exchange resin
4. Weak anion exchange resin
According to the Source they can -
Natural resins : Cation - Zeolytes, Clay
Anion - Dolomite
Synthetic resins: Inorganic & Organic resins
◘Organic resins are polymeric resin matrix.
The resin composed of –
Polystyrene (sites for exchangeable functional groups)
Divinyl benzene(Cross linking agent)-offers stability.
Ion exchange resin should have following requirements
»It must be chemically stable.
»It should be insoluble in common solvents.
» It should have a sufficient degree of cross linking.
»The swollen resin must be denser than water.
»It must contain sufficient no. of ion exchange groups.
Physical properties of ion exchange resins
Cross linking:
It affects swelling & strength & solubility
Swelling:
When resin swells, polymer chain spreads apart
Polar solvents → swelling
Non-polar solvents → contraction
Swelling also affected electrolyte concentration.
Particle size and porosity
Increase in surface area & decrease in particle size will increase the rate of ion exchange.
Regeneration
Cation exchange resin are regenerated by treatment with acid, then washing with water.
Anion exchange resin are regenerated by treatment with NaOH, then washing with water until neutral.
EXPERIMENTAL SETUP OF ION EXCHANGE CHROMATOGRAPHY
Metrohm 850 Ion chromatography system
Instrumentation of ion exchange chromatography
PRACTICAL REQUIREMENTS
1.Column
» glass, stainless steel or polymers
2.Packing the column
» Wet packing method:
A slurry is prepared of the eluent with the stationary phase powder and then carefully poured into the column. Care must be taken to avoid air bubbles.
3.Application of the sample
After packing, sample is added to the top of the stationary phase, use syringe or pipette.
This layer is usually topped with a small layer of sand or with cotton or glass wool to protect the shape of the organic layer from the velocity of newly added eluent.
4.Mobile phase
Acids, alkalis, buffers…
6.Stationary phase
The ionic
Electrophoresis is the movement of charged particles through an electrode when subjected to an electric Field
Cations move towards cathode
Anions move towards anode
By this technique solutes are separated by their different rates of travel through an electric field.
Commonly used in biological analysis, particularly in the separations of proteins, peptides and nucleic acids
The technique of paper electrophoresis is simple and inexpensive and requires only micro quantities of plasma for separation.
The support medium is a filter paper
The electrophoresis apparatus in its simplest form consists of two troughs to contain buffer solution, through which electric current is passed.
Frequently used in isolating proteins, amino acids and oligopeptides.
In this slide contains types, working principle, factors affecting, advantage and disadvantage of paper electrophoresis.
Presented by: G.Sai Swetha. (Department of pharmacology),
RIPER, anantapur.
It is a subtype of the gel electrophoresis whereby the normal gel is replaced with polyacrylamide gels used as support media.
Gels are made by free radical-induced polymerization of acrylamide and N,N’-Methylenebisacrylamide.
It is the most widely used technique of electrophoresis.
Isoelectric focusing electrophoresis- Principle , procedure and applicationsJaskiranKaur72
IEF separates amphoteric compounds, such as proteins, with increased resolution in a medium possessing a stable pH gradient. The protein becomes “focused” at a point on the gel as it migrates to a zone where the pH of the gel matches the protein's pI. At this point, the charge of the protein becomes zero and its migration ceases.
ION EXCHANGE CHROMATOGRAPHY
ByM.Vharshini
B.Sc. Bio Medical Science
Sri Ramachandra University
ION EXCHANGE CHROMATOGRAPHY
Ion-exchange chromatography is a process that allows the separation of ions and polar molecules based on their affinity to the ion exchanger.
It can be used for almost any kind of charged molecule including large proteins, small nucleotides and amino acids.
Cations or Anions can be separated using this method.
PRINCIPLE
It is based on the reversible electrostatic interaction of ions with the separation matrix (i.e.)
The separation occurs by reversible exchange of ions between the ions present in the solution and those present in the ion exchange resin.
CLASSIFICATION OF RESINS
According to the chemical nature they classified as-
1. Strong cation exchange resin
2. Weak cation exchange resin
3. Strong anion exchange resin
4. Weak anion exchange resin
According to the Source they can -
Natural resins : Cation - Zeolytes, Clay
Anion - Dolomite
Synthetic resins: Inorganic & Organic resins
◘Organic resins are polymeric resin matrix.
The resin composed of –
Polystyrene (sites for exchangeable functional groups)
Divinyl benzene(Cross linking agent)-offers stability.
Ion exchange resin should have following requirements
»It must be chemically stable.
»It should be insoluble in common solvents.
» It should have a sufficient degree of cross linking.
»The swollen resin must be denser than water.
»It must contain sufficient no. of ion exchange groups.
Physical properties of ion exchange resins
Cross linking:
It affects swelling & strength & solubility
Swelling:
When resin swells, polymer chain spreads apart
Polar solvents → swelling
Non-polar solvents → contraction
Swelling also affected electrolyte concentration.
Particle size and porosity
Increase in surface area & decrease in particle size will increase the rate of ion exchange.
Regeneration
Cation exchange resin are regenerated by treatment with acid, then washing with water.
Anion exchange resin are regenerated by treatment with NaOH, then washing with water until neutral.
EXPERIMENTAL SETUP OF ION EXCHANGE CHROMATOGRAPHY
Metrohm 850 Ion chromatography system
Instrumentation of ion exchange chromatography
PRACTICAL REQUIREMENTS
1.Column
» glass, stainless steel or polymers
2.Packing the column
» Wet packing method:
A slurry is prepared of the eluent with the stationary phase powder and then carefully poured into the column. Care must be taken to avoid air bubbles.
3.Application of the sample
After packing, sample is added to the top of the stationary phase, use syringe or pipette.
This layer is usually topped with a small layer of sand or with cotton or glass wool to protect the shape of the organic layer from the velocity of newly added eluent.
4.Mobile phase
Acids, alkalis, buffers…
6.Stationary phase
The ionic
Electrophoresis is the movement of charged particles through an electrode when subjected to an electric Field
Cations move towards cathode
Anions move towards anode
By this technique solutes are separated by their different rates of travel through an electric field.
Commonly used in biological analysis, particularly in the separations of proteins, peptides and nucleic acids
Sodium dodecyl sulphate - Polyacrylamide Gel Electrophoresis (SDS - PAGE) is a technique used for the separation of deoxyribonucleic acid (DNA) ,Ribonucleic acid (RNA) And protein molecules according to their size and electrical charge.
Electrophoresis is a laboratory technique used to separate DNA, RNA, or protein molecules based on their size and electrical charge. An electric current is used to move molecules to be separated through a gel. Pores in the gel work like a sieve, allowing smaller molecules to move faster than larger molecules.
Electrophoresis is a laboratory technique used to separate DNA, RNA, or protein molecules based on their size and electrical charge.
Different types of electrophoresis.
Gel electrophoresis; Agarose Gel electrophoresis; polyacrylamide gel electrophoresis; pulsed-field gel electrophoresis
This presentation includes the principle involved, chemistry, procedure, and application of various advance molecular biology like SDS PAGE, Western Blotting, and ELISA.
SDS PAGE is widely used to analyze the proteins in complex extracts.
The polyacrylamide gels are used to separate proteins.
Polyacrylamide is inert, and hence, shows no interaction with the protein being separated and forms a matrix.
Size of the pores in the gel can be controlled by adjusting the concentration of acrylamide.
Acrylamide undergoes polymerization in order to form a gel. Hence, APS (ammonium per sulphate) & TEMED (N,N,N’,N’-tetramethylethylenediamine) are added to initiate the process of polymerization.
It's application includes separation of protein mixture on separating gel and their identification using different techniques like western blotting.
Western blotting, also known as immunoblotting or protein blotting, is a core technique in cell and molecular biology. In most basic terms, it is used to detect the presence of a specific protein in a complex mixture extracted from cells.
Western blots are effective in detecting low nanogram to low picogram amounts of target protein, depending on the antibodies used and the detection substrate chosen. If the target is suspected to be of very low abundance, or if there is no detectible signal on the blot, then it may be necessary to concentrate, immunoprecipitate, or fractionate the starting material.
This technique is used to study cell signalling pathways, cell cycle pathways, drug action pathways, protein-protein interaction.
ELISA (enzyme-linked immunosorbent assay) is a plate-based assay technique designed for detecting and quantifying peptides, proteins, antibodies, and hormones.
In an ELISA, an antigen must be immobilized to a solid surface and then complexed with an antibody that is linked to an enzyme.
Detection is accomplished by assessing the conjugated enzyme activity via incubation with a substrate to produce a measurable product.
The most crucial element of the detection strategy is a highly specific antibody-antigen interaction.
ELISA begins with a coating step, in which the first layer, consisting of a target antigen or antibody, is adsorbed onto a 96-well polystyrene plate.
This is followed by a blocking step in which all unbound sites are coated with a blocking agent.
Following a series of washes, the plate is incubated with enzyme-conjugated antibody.
Another series of washes removes all unbound antibody.
A substrate is then added, producing a calorimetric signal. Finally, the plate is read.
It's types include Direct ELISA, Indirect ELISA, Sandwich ELISA and competitive ELISA. This technique is used to determine serum antibody concentrations, potential food allergens (milk, peanuts, almonds), detection of antigens and antibodies, disease outbreaks.
Essential Textbook of Biochemistry For Nursing (B.Sc.Nursing & PBN)Tapeshwar Yadav
I have relished teaching Biochemistry during my more than Ten years teaching experience in a medical, dental, nursing and health science colleges. It was because of constant inspiration from my students that I could come up with Essentials Textbook of Biochemistry for Nursing book, which hopefully would meet the inadequacies the students face in other books. In this age when the concepts in this subject are constantly changing, this book attempts to summarise the fundamentals and current state of knowledge in Biochemistry.
Biochemistry has been primarily written for the students of B.Sc. Nursing & Post Basic of Nursing (PBN) in such a way that it will also be suitable for General Medicine, Radiography, Physiotherapy, Ayurveda, Optometry, Dental and Nursing. This book can also be used as Reference for B.Sc. MLT, Bachelor of Pharmacy (B. PHARMA), Bachelor of Public Health (BPH), Bachelor of Physiotherapy (BPT), B. Ophthalmology, Bachelor of Radiography (BRT) and Biomedical Engineering students of Tribhuvan University, Purbanchal University, Kathmandu University and Pokhara University. Similarly, it will be equally useful for all the teachers, academic writers and those who are involved directly or indirectly in teaching and practising Health Sciences.
This is a basic book on Essential Textbook of Biochemistry for Nursing. The book thoroughly discusses some of the major concepts of Biochemistry and provides adequate information to help the students understand its implications in various areas of the subject. Furthermore, the book aims at equipping the students with practical cum theoretical skills. The book covers almost all the topics which have been prescribed in the Syllabus.
This is an introductory course to Biochemistry and is about medical biochemistry including the biochemical processes of - digestion & absorption of foods, metabolism of different kinds of foods & their disturbance effects in our body together with the physiological roles of different kinds of vitamins & enzymes.
The book consists of Theory as well as Practical portion. The author has tried his best to make all the concepts of each unit as lucid and simple as required for the students with supportive examples, samples, diagrams, clinical disorders and practical works. The ultimate purpose of this book is to equip the reader with comprehensive knowledge in Biochemistry with reference to basic as well as clinical aspects.
At last, I have made every effort to make the book error free, I am under no illusion. I expect constructive comments and suggestions from learners and teachers who use this book which will obviously help me in improving the future edition of the book.
Amino acids are a group of organic compounds containing two functional groups amino and carboxyl. The amino group (-NH2) is basic while the carboxyl group (-COOH) is acidic in nature.
The plasma in the liquid medium of blood (55%) in which the cell components namely Erythrocytes, Leucocytes and Platelets are suspended.
If anticoagulated blood is centrifuged, the plasma separates out as a supernatant while the cells remain at the bottom.
Plasma consists of water electrolytes metabolites nutrients proteins and hormones.
Most of the plasma proteins are synthesized in the liver.
Plasma proteins are separated by electrophoresis.
The word protein is derived from the Greek word ‘Proteios’ which means holding the first place. Berzelius (Swedish chemist) suggested the name proteins to the group of organic compounds that are important to life.
Proteins are the most abundant organic molecules of the living system.
They occur in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life.
Out of the total dry body weight, 3/4th are made up of proteins.
Proteins are used for body building; all the major structural and functional aspects of the body are carried out by protein molecules.
Proteins are high molecular weight polypeptides containing α-amino acids joined together by peptide linkage (-CO-NH).
The endocrine system consists of a network of ductless glands that secrete chemicals (called hormones) that affect the function of specific organs within the body, thus regulating many of the intricate functions of the body itself.
These ductless glands secrete their hormones directly into the bloodstream, as opposed to releasing them externally through ducts (as do the sweat glands and the oil glands).
The field of medicine that deals with the study of the endocrine system and the treatment of the diseases and disorders of the endocrine system is known as endocrinology.
The physician who specializes in the medical practice of endocrinology
is known as an endocrinologist.
Carbohydrates are the most abundant organic molecules in nature.
They are commonly known as saccharides or sugars.
They are primarily composed of the elements carbon, hydrogen and oxygen.
The name carbohydrate literally means “hydrates of carbon”.
Carbohydrates are widely distributed in nature in plants and animals.
The most important carbohydrate found in plants is starch.
It occurs abundantly in roots, tubers, vegetables and grains. The carbohydrate found in animals is glycogen.
It is a storage form of carbohydrate present in liver and muscles, which serves as important sources of energy for vital activities.
This field combines biology as well as chemistry to study the chemical structure of a living organism
Biochemistry is a basic science which deals with chemical nature and chemical behaviour of living matter and with the reactions and processes they undergo.
“The branch of science dealing with the study of all the life processes such as control and coordination within a living organism is called Biochemistry”
Medical parasitology : study of parasites that infect human, diseases caused by them, clinical picture, their diagnosis, treatment and prevention as well as controls.
It involves drug development, epidemiological studies and study of zoonoses.
To know various terms related to parasitology.
To know about general parasites and parasitic infections.
To get knowledge about laboratory diagnosis and its importance.
To gain idea about general epidemiological aspects of parasites that affect human.
Apply basic methods of specimen collection , preservation and processing in lab.
To prevent ourselves from these infections and apply control measures.
Microbiology is the study of
living organisms of microscopic
size which includes bacteria ,
Fungi , Algae , Protozoa and Viruses. It is concerned with the forms, structure , reproduction , physiology , metabolism and classification.
Principle Of Microbiology
Medical microbiology deals with the causative agent of the infectious disease of the human , the ways in which they produce disease in the body and essential information for diagnosis and treatment.
Hematology is the branch of medicine, that is concerned with the study of blood, blood forming organs and blood diseases. It includes study of etiology, diagnosis, treatment, prognosis and prevention of blood diseases .
After the completion of this presentation we will know about:
What is hematology and its purpose.
hematology laboratory.
Blood and its compositions and collections
Hematology lab equipment's
Some hematological tests , disease and hazards too.
Biochemistry is the study of the structure and function of biological molecules such as proteins, nucleic acids, carbohydrates and lipids.
Biochemistry is the study of the chemistry of living things. This includes organic molecules and their chemical reactions.
Biochemistry deals with body substance like enzymes, carbohydrates, amino acids, fats, proteins, hormones, DNA, RNA, pigments etc.
The major objective of biochemistry is the complete understanding of all chemical processes associated with living cells at the molecular level. Some of the objectives can be listed as follows:
1. Isolation, structural elucidation and the determination of mode of action of biomolecules.
2. Identification of disease mechanisms.
3. Study of in born errors of metabolism.
4. Study of oncogenes in cancer cells.
5. The relationship of biochemistry with the genetics, physiology, immunology, pharmacology, toxicology etc.
Biochemistry is related to almost all the life sciences and without biochemistry background and knowledge, a through understanding of health and well-being is not possible.
It is a well known fact that metal ions have a profound effect on cellular processes
The importance or the role that ions play in cellular activity can be gauged by the fact that most cells maintain a very critical Na+ & k+ balance between the extracellular and the intracellular spaces.
Any distribution in this critical balance is to the cellular metabolism through a drastic change in the osmotic pressure resulting in cellular swelling.
An ISE operates an exactly the same principles as a PH electrode
In fact, a PH electrode is a type of ion selective electrode sensitive to hydrogen ion.
Just like a PH electrode, the electrode body contains a reference solution and an metal reference electrode
Safety cabinets are intended to protect a laboratory worker from aerosols and airborne particles.
They will not protect the person from spillages and the consequences of mishandling and poor technique.
Aerosol particles of less than 5 µm in diameter and small droplets of 5–100 µm in diameter are not visible to the naked eye.
The laboratory worker is generally not aware that such particles are being generated and may be inhaled or may cross contaminate work surface materials.
BSCs, when properly used, have been shown to be highly effective in reducing laboratory-acquired infections and cross-contaminations of cultures due to aerosol exposures. BSCs also protect the environment.
Most BSCs use high efficiency particulate air (HEPA) filters in the exhaust and supply systems.
The exception is a Class I BSC, which does not have HEPA filtered supply air.
The application of knowledge, techniques and equipment to prevent a personal laboratory and environmental exposure to potentially infectious agents or biohazard is known as biosafety.
Biosafety defines the containment conditions under which infectious agents can be safely manipulated.
The objective of containment is to confine biohazard and to reduce the potential exposure of the laboratory worker, persons outside of the laboratory, and the environment to potentially infectious agents.
A pipette (also called a point or a pipettor) is a laboratory instrument used to transfer a measured volume of liquid.
Pipettes are commonly used in chemistry and molecular biology research as well as clinical biochemistry tests.
Pipettes come in several designs for various purposes with different levels of accuracy and precision, from single piece flexible plastic transfer pipettes to more complex adjustable or electronic pipettes.
A pipette works by creating a vacuum above the liquid-holding chamber and selectively releasing this vacuum to draw and dispense liquid.
Safe Use and Storage of Chemicals and ReagentsTapeshwar Yadav
Even in the smallest laboratory, dangerous chemicals are used directly or incorporated into stains and reagents.
Hence the correct handling and storage of hazardous chemicals is essential to prevent injury and damage.
In addition to this, to reduce accidents caused by chemicals, labeling is very important.
Laboratory Hazards, Accidents and Safety RulesTapeshwar Yadav
Injury, damage and loss by fire can be minimized when laboratory staff:
Understand how fires are caused and spread;
Reduce the risk of fire by following fire safety regulations at all times;
Know what to do if there is a fire in their laboratory;
Know how to use fire fighting equipment;
Know how to apply emergency First Aid, for burns.
Revised Curriculum of Certificate in Medical Laboratory Technology(CMLT) by C...Tapeshwar Yadav
This curriculum of 3 years Certificate in Medical Laboratory Technology is designed to produce middle level skilled laboratory personnel equipped with knowledge, skills and attitudes of medical laboratory with a view to provide diagnostic, curative, preventive and promotive laboratory services to the community. Such technicians collect specimens, process, and perform tests to analyze body fluids, tissue, and other substances. The graduates perform lab procedures and maintain instruments. The graduates are expected to perform tests that help other healthcare professionals such as physicians to detect, diagnose, and treat diseases.
The program extends over three academic years. The first year course focuses on basic science and foundational subjects, the second year course focuses on theory and practical parts of basic medical laboratory subjects. Simultaneously the third year is given to the application of learned skills and knowledge in the comprehensive practical settings, in hospitals and medical laboratory. The graduates will have career opportunities in hospitals, diagnostic laboratories, clinics, industry and physicians' offices, research centers, blood bank, crime investigating laboratories etc. It is based on the code of conduct of Nepal Health professional Council.
Clinical Pathology is the application of laboratory techniques to find out the cause of disease. Clinical pathology laboratory involves all aspect of the medicine ranging from the field of biochemistry, microbiology, Parasitology, haematology, immunology and cytogenetics etc. Clinical pathology laboratory perform qualitative and quantitative analysis of body fluid such as urine, blood, CSF, sputum, other body fluid such as synovial fluid, peritoneal fluid, pericardial fluid and plural fluid. These determinations are useful in diagnosing various clinical conditions such as diabetes mellitus, jaundice, gout, hyperlipidemia, pancreatitis, rickets, etc. The clinical pathological tests are very useful in determining the severity of diseases of many organs such as liver, stomach, heart, kidneys, brain as well as the endocrine disorders and related status of acid-base balance of the body. The clinical pathology tests, in relation to the various clinical conditions can be applicable for:-
1) Reveal the causes of the diseases
2) Screen easy diagnosis
3) Suggest effective treatment
4) Assist in monitoring progress of a pathological condition and
5) Help in assessing response to therapy
Modern medicine says that: Your practice of medicine will be as good as your understanding of pathology.
- Video recording of this lecture in English language: https://youtu.be/lK81BzxMqdo
- Video recording of this lecture in Arabic language: https://youtu.be/Ve4P0COk9OI
- Link to download the book free: https://nephrotube.blogspot.com/p/nephrotube-nephrology-books.html
- Link to NephroTube website: www.NephroTube.com
- Link to NephroTube social media accounts: https://nephrotube.blogspot.com/p/join-nephrotube-on-social-media.html
Report Back from SGO 2024: What’s the Latest in Cervical Cancer?bkling
Are you curious about what’s new in cervical cancer research or unsure what the findings mean? Join Dr. Emily Ko, a gynecologic oncologist at Penn Medicine, to learn about the latest updates from the Society of Gynecologic Oncology (SGO) 2024 Annual Meeting on Women’s Cancer. Dr. Ko will discuss what the research presented at the conference means for you and answer your questions about the new developments.
Lung Cancer: Artificial Intelligence, Synergetics, Complex System Analysis, S...Oleg Kshivets
RESULTS: Overall life span (LS) was 2252.1±1742.5 days and cumulative 5-year survival (5YS) reached 73.2%, 10 years – 64.8%, 20 years – 42.5%. 513 LCP lived more than 5 years (LS=3124.6±1525.6 days), 148 LCP – more than 10 years (LS=5054.4±1504.1 days).199 LCP died because of LC (LS=562.7±374.5 days). 5YS of LCP after bi/lobectomies was significantly superior in comparison with LCP after pneumonectomies (78.1% vs.63.7%, P=0.00001 by log-rank test). AT significantly improved 5YS (66.3% vs. 34.8%) (P=0.00000 by log-rank test) only for LCP with N1-2. Cox modeling displayed that 5YS of LCP significantly depended on: phase transition (PT) early-invasive LC in terms of synergetics, PT N0—N12, cell ratio factors (ratio between cancer cells- CC and blood cells subpopulations), G1-3, histology, glucose, AT, blood cell circuit, prothrombin index, heparin tolerance, recalcification time (P=0.000-0.038). Neural networks, genetic algorithm selection and bootstrap simulation revealed relationships between 5YS and PT early-invasive LC (rank=1), PT N0—N12 (rank=2), thrombocytes/CC (3), erythrocytes/CC (4), eosinophils/CC (5), healthy cells/CC (6), lymphocytes/CC (7), segmented neutrophils/CC (8), stick neutrophils/CC (9), monocytes/CC (10); leucocytes/CC (11). Correct prediction of 5YS was 100% by neural networks computing (area under ROC curve=1.0; error=0.0).
CONCLUSIONS: 5YS of LCP after radical procedures significantly depended on: 1) PT early-invasive cancer; 2) PT N0--N12; 3) cell ratio factors; 4) blood cell circuit; 5) biochemical factors; 6) hemostasis system; 7) AT; 8) LC characteristics; 9) LC cell dynamics; 10) surgery type: lobectomy/pneumonectomy; 11) anthropometric data. Optimal diagnosis and treatment strategies for LC are: 1) screening and early detection of LC; 2) availability of experienced thoracic surgeons because of complexity of radical procedures; 3) aggressive en block surgery and adequate lymph node dissection for completeness; 4) precise prediction; 5) adjuvant chemoimmunoradiotherapy for LCP with unfavorable prognosis.
Tom Selleck Health: A Comprehensive Look at the Iconic Actor’s Wellness Journeygreendigital
Tom Selleck, an enduring figure in Hollywood. has captivated audiences for decades with his rugged charm, iconic moustache. and memorable roles in television and film. From his breakout role as Thomas Magnum in Magnum P.I. to his current portrayal of Frank Reagan in Blue Bloods. Selleck's career has spanned over 50 years. But beyond his professional achievements. fans have often been curious about Tom Selleck Health. especially as he has aged in the public eye.
Follow us on: Pinterest
Introduction
Many have been interested in Tom Selleck health. not only because of his enduring presence on screen but also because of the challenges. and lifestyle choices he has faced and made over the years. This article delves into the various aspects of Tom Selleck health. exploring his fitness regimen, diet, mental health. and the challenges he has encountered as he ages. We'll look at how he maintains his well-being. the health issues he has faced, and his approach to ageing .
Early Life and Career
Childhood and Athletic Beginnings
Tom Selleck was born on January 29, 1945, in Detroit, Michigan, and grew up in Sherman Oaks, California. From an early age, he was involved in sports, particularly basketball. which played a significant role in his physical development. His athletic pursuits continued into college. where he attended the University of Southern California (USC) on a basketball scholarship. This early involvement in sports laid a strong foundation for his physical health and disciplined lifestyle.
Transition to Acting
Selleck's transition from an athlete to an actor came with its physical demands. His first significant role in "Magnum P.I." required him to perform various stunts and maintain a fit appearance. This role, which he played from 1980 to 1988. necessitated a rigorous fitness routine to meet the show's demands. setting the stage for his long-term commitment to health and wellness.
Fitness Regimen
Workout Routine
Tom Selleck health and fitness regimen has evolved. adapting to his changing roles and age. During his "Magnum, P.I." days. Selleck's workouts were intense and focused on building and maintaining muscle mass. His routine included weightlifting, cardiovascular exercises. and specific training for the stunts he performed on the show.
Selleck adjusted his fitness routine as he aged to suit his body's needs. Today, his workouts focus on maintaining flexibility, strength, and cardiovascular health. He incorporates low-impact exercises such as swimming, walking, and light weightlifting. This balanced approach helps him stay fit without putting undue strain on his joints and muscles.
Importance of Flexibility and Mobility
In recent years, Selleck has emphasized the importance of flexibility and mobility in his fitness regimen. Understanding the natural decline in muscle mass and joint flexibility with age. he includes stretching and yoga in his routine. These practices help prevent injuries, improve posture, and maintain mobilit
ARTIFICIAL INTELLIGENCE IN HEALTHCARE.pdfAnujkumaranit
Artificial intelligence (AI) refers to the simulation of human intelligence processes by machines, especially computer systems. It encompasses tasks such as learning, reasoning, problem-solving, perception, and language understanding. AI technologies are revolutionizing various fields, from healthcare to finance, by enabling machines to perform tasks that typically require human intelligence.
These lecture slides, by Dr Sidra Arshad, offer a quick overview of physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar leads (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
Pulmonary Thromboembolism - etilogy, types, medical- Surgical and nursing man...VarunMahajani
Disruption of blood supply to lung alveoli due to blockage of one or more pulmonary blood vessels is called as Pulmonary thromboembolism. In this presentation we will discuss its causes, types and its management in depth.
Prix Galien International 2024 Forum ProgramLevi Shapiro
June 20, 2024, Prix Galien International and Jerusalem Ethics Forum in ROME. Detailed agenda including panels:
- ADVANCES IN CARDIOLOGY: A NEW PARADIGM IS COMING
- WOMEN’S HEALTH: FERTILITY PRESERVATION
- WHAT’S NEW IN THE TREATMENT OF INFECTIOUS,
ONCOLOGICAL AND INFLAMMATORY SKIN DISEASES?
- ARTIFICIAL INTELLIGENCE AND ETHICS
- GENE THERAPY
- BEYOND BORDERS: GLOBAL INITIATIVES FOR DEMOCRATIZING LIFE SCIENCE TECHNOLOGIES AND PROMOTING ACCESS TO HEALTHCARE
- ETHICAL CHALLENGES IN LIFE SCIENCES
- Prix Galien International Awards Ceremony
Explore natural remedies for syphilis treatment in Singapore. Discover alternative therapies, herbal remedies, and lifestyle changes that may complement conventional treatments. Learn about holistic approaches to managing syphilis symptoms and supporting overall health.
Title: Sense of Taste
Presenter: Dr. Faiza, Assistant Professor of Physiology
Qualifications:
MBBS (Best Graduate, AIMC Lahore)
FCPS Physiology
ICMT, CHPE, DHPE (STMU)
MPH (GC University, Faisalabad)
MBA (Virtual University of Pakistan)
Learning Objectives:
Describe the structure and function of taste buds.
Describe the relationship between the taste threshold and taste index of common substances.
Explain the chemical basis and signal transduction of taste perception for each type of primary taste sensation.
Recognize different abnormalities of taste perception and their causes.
Key Topics:
Significance of Taste Sensation:
Differentiation between pleasant and harmful food
Influence on behavior
Selection of food based on metabolic needs
Receptors of Taste:
Taste buds on the tongue
Influence of sense of smell, texture of food, and pain stimulation (e.g., by pepper)
Primary and Secondary Taste Sensations:
Primary taste sensations: Sweet, Sour, Salty, Bitter, Umami
Chemical basis and signal transduction mechanisms for each taste
Taste Threshold and Index:
Taste threshold values for Sweet (sucrose), Salty (NaCl), Sour (HCl), and Bitter (Quinine)
Taste index relationship: Inversely proportional to taste threshold
Taste Blindness:
Inability to taste certain substances, particularly thiourea compounds
Example: Phenylthiocarbamide
Structure and Function of Taste Buds:
Composition: Epithelial cells, Sustentacular/Supporting cells, Taste cells, Basal cells
Features: Taste pores, Taste hairs/microvilli, and Taste nerve fibers
Location of Taste Buds:
Found in papillae of the tongue (Fungiform, Circumvallate, Foliate)
Also present on the palate, tonsillar pillars, epiglottis, and proximal esophagus
Mechanism of Taste Stimulation:
Interaction of taste substances with receptors on microvilli
Signal transduction pathways for Umami, Sweet, Bitter, Sour, and Salty tastes
Taste Sensitivity and Adaptation:
Decrease in sensitivity with age
Rapid adaptation of taste sensation
Role of Saliva in Taste:
Dissolution of tastants to reach receptors
Washing away the stimulus
Taste Preferences and Aversions:
Mechanisms behind taste preference and aversion
Influence of receptors and neural pathways
Impact of Sensory Nerve Damage:
Degeneration of taste buds if the sensory nerve fiber is cut
Abnormalities of Taste Detection:
Conditions: Ageusia, Hypogeusia, Dysgeusia (parageusia)
Causes: Nerve damage, neurological disorders, infections, poor oral hygiene, adverse drug effects, deficiencies, aging, tobacco use, altered neurotransmitter levels
Neurotransmitters and Taste Threshold:
Effects of serotonin (5-HT) and norepinephrine (NE) on taste sensitivity
Supertasters:
25% of the population with heightened sensitivity to taste, especially bitterness
Increased number of fungiform papillae
HOT NEW PRODUCT! BIG SALES FAST SHIPPING NOW FROM CHINA!! EU KU DB BK substit...GL Anaacs
Contact us if you are interested:
Email / Skype : kefaya1771@gmail.com
Threema: PXHY5PDH
New BATCH Ku !!! MUCH IN DEMAND FAST SALE EVERY BATCH HAPPY GOOD EFFECT BIG BATCH !
Contact me on Threema or skype to start big business!!
Hot-sale products:
NEW HOT EUTYLONE WHITE CRYSTAL!!
5cl-adba precursor (semi finished )
5cl-adba raw materials
ADBB precursor (semi finished )
ADBB raw materials
APVP powder
5fadb/4f-adb
Jwh018 / Jwh210
Eutylone crystal
Protonitazene (hydrochloride) CAS: 119276-01-6
Flubrotizolam CAS: 57801-95-3
Metonitazene CAS: 14680-51-4
Payment terms: Western Union,MoneyGram,Bitcoin or USDT.
Deliver Time: Usually 7-15days
Shipping method: FedEx, TNT, DHL,UPS etc.Our deliveries are 100% safe, fast, reliable and discreet.
Samples will be sent for your evaluation!If you are interested in, please contact me, let's talk details.
We specializes in exporting high quality Research chemical, medical intermediate, Pharmaceutical chemicals and so on. Products are exported to USA, Canada, France, Korea, Japan,Russia, Southeast Asia and other countries.
Anti ulcer drugs and their Advance pharmacology ||
Anti-ulcer drugs are medications used to prevent and treat ulcers in the stomach and upper part of the small intestine (duodenal ulcers). These ulcers are often caused by an imbalance between stomach acid and the mucosal lining, which protects the stomach lining.
||Scope: Overview of various classes of anti-ulcer drugs, their mechanisms of action, indications, side effects, and clinical considerations.
2. 2
IntroductionIntroduction
Separation is brought about through molecular sieving
technique, based on the molecular size of the substances.
Gel material acts as a "molecular sieve”.
Gel is a colloid in a solid form (99% is water).
It is important that the support media is electrically
neutral.
Different types of gels which can be used are; Agar and
Agarose gel, Starch, Sephadex, Polyacrylamide gels.
3. 3
Contd…Contd…
A porous gel acts as a sieve by retarding or, in some
cases, by completely obstructing the movement of
macromolecules while allowing smaller molecules to
migrate freely.
Agar gel is used for separation of different types of
protein mixtures as well as nucleic acids
Polyacrylamide is most suitable for separation of
nucleic acids. It is also frequently used in separating
proteins, peptides and amino acids from microgram
quantities of mixed samples
7. Gel Types
Polysaccharide extracted
from sea weed.
Gel casted horizontally
Non-toxic.
Separate large molecules
Commonly used for DNA
separations.
Staining can be done before
or pouring the gel.
Cross-linked polymer of
acrylamide.
Gel casted vertically.
Potent neuro-toxic.
Separate small molecules.
Used for DNA or protein
separations.
Staining can be done after
pouring the gel.
Agarose Polyacrylamide Gel
8. Agarose gel electrophoresis
Commonly used support medium
Less expensive than cellulose acetate
Equally good separation
Agar is a complex acidic polysaccharide containing monomers of
sulfated galactose
Agarose is a sulfate free fraction of Agar
Gel is prepared in buffer and spread over a microscopic slide
A small sample of serum or biological fluid is applied by cutting
in to the gel with a sharp edge
The electrophoretic rum takes about 90 minutes
8
9. 9
Agar is a mixture of poly saccharides extracted from
sea weeds.
Agarose is a highly purified uncharged
polysaccharide derived from agar.
Agarose is chemically basic disaccharide repeating
units of 3,6-anhydro-L-galactose.
Agarose dissolves when added to boiling liquid. It
remains in a liquid state until the temperature is lowered to
about 40° C at which point it gels.
AGAR AND AGAROSE GELAGAR AND AGAROSE GEL
10. 10
The pore size may be predetermined by adjusting
the concentration of agarose in the gel.
Agarose gels are fragile. They are actually
hydrocolloids, and they are held together by the
formation of weak hydrogen and hydrophobic
bonds.
The pores of an agarose gel are large, agarose is
used to separate macromolecules such as nucleic
acids, large proteins and protein complexes.
11. 11
ADVANTAGES:ADVANTAGES:
Easy to prepare and small concentration of agar is required.
Resolution is superior to that of filter paper.
Large quantities of proteins can be separated and recovered.
Adsorption of negatively charged protein molecule is
negligible.
It adsorbs proteins relatively less when compared to other
medium.
Sharp zones are obtained due to less adsorption.
Recovery of protein is good, good method for preparative
purpose.
12. 12
DISADVANTAGES:DISADVANTAGES:
Electro osmosis is high.
Resolution is less compared to polyacrylamide gels.
Different sources and batches of agar tend to give different
results and purification is often necessary.
APPLICATION:APPLICATION:
Widely used in Immuno electrophoresis.
To separate different types of protein mixtures as well as
nucleic acids.
14. It is prepared by polymerizing acryl amide
monomers in the presence of methylene-bis-
acrylamide to cross link the monomers.
•Structure of acrylamide (CH2=CH-CO-NH2)
•Polyacrylamide gel structure held together by
covalent cross-links.
•Polyacrylamide gels are tougher than agarose gels.
•It is thermostable, transparent, strong and relatively
chemically inert.
•Gels are uncharged and are prepared in a variety of pore
sizes.
•Proteins are separated on the basis of charge to
mass ratio and molecular size, a phenomenon
called Molecular sieving.
POLYACRYLAMIDE GEL ELECTROPHORESIS
(PAGE)
14
15. TTypes ofypes of PAGEPAGE
15
PAGE can be classified according the separation conditions into:
NATIVE-PAGE:
Native gels are run in non-denaturing conditions, so that the analyte's natural
structure is maintained.
Separation is based upon charge, size, and shape of macromolecules.
Useful for separation or purification of mixture of proteins.
This was the original mode of electrophoresis.
DENATURED-PAGE OR SDS-PAGE:
Separation is based upon the molecular weight of proteins.
The common method for determining MW of proteins.
Very useful for checking purity of protein samples.
16. PAGE-ProcedurePAGE-Procedure
16
The gel of different pore sizes is cast into a column inside a vertical tube,
often with large pore gel at the top and small pore gel at the bottom.
Microgram quantity of the sample is placed over the top of the gel column
and covered by a buffer solution having such a pH so as to change sample
components into anions.
The foot of the gel column is made to dip in the same buffer in the bottom
reservoir.
Cathode and anode are kept above and below the column to impose an
electric field through the column.
17. PAGE-ProcedurePAGE-Procedure
17
Macromolecular anions move towards the anode down the
gel column.
There is no external solvent space, all the migratory
particles have to pass through the gel pores.
Rate of migration depends on the charge to mass ratio.
Different sample components get separated into discrete
migratory bands along the gel column on the basis of
electrophoretic mobility and gel filtration effect.
19. 19
Polyacrylamide Gel Electrophoresis
(PAGE)
a) The gel is poured vertically
between two glass plates.
b.) Protein bands are separated on the
basis of relative molecular weight and
visualized with stains.
SLAB PAGESLAB PAGEPAGE PROCEDUREPAGE PROCEDURE
20. Visualization
After the electrophoresis is complete, the molecules in the gel
can be stained to make them visible.
Ethidium bromide, silver, or coomassie blue dye may be used
for this process.
Other methods may also be used to visualize the separation of
the mixture's components on the gel.
If the analyte molecules fluoresce under ultraviolet light, a
photograph can be taken of the gel under ultraviolet lighting
conditions. If the molecules to be separated contain radioactivity
added for visibility, an autoradiogram can be recorded of the gel.
22. SDS-PAGESDS-PAGE
SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel
electrophoresis, is a technique widely used in biochemistry, forensics,
genetics and molecular biology to separate proteins according to their
electrophoretic mobility.
When a detergent SDS added to PAGE the combined procedure is
termed as SDS PAGE.
SDS coats protein molecules giving all proteins a constant charge-
mass ratio.
Due to masking of charges of proteins by the large negative charge
on SDS binding with them, the proteins migrate along the gel in
order of increasing sizes or molecular weights.
22
23. SDS is an anionic detergent which denatures secondary and non–
disulfide–linked tertiary structures by wrapping around the
polypeptide backbone. In so doing, SDS confers a net negative
charge to the polypeptide in proportion to its length.
Molecules in solution with SDS have a net negative charge within a
wide pH range.
A polypeptide chain binds amounts of SDS in proportion to its
relative molecular mass.
The negative charges on SDS destroy most of the complex structure
of proteins, and are strongly attracted toward an anode in an electric
field.23
26. Sds-coated large proteins migrate slowly through the gel matrix
and small proteins migrate quickly through the matrix
The nearer the band to the well, the larger the molecular size of
protein
27.
28. Differences
• Separation is based upon
charge, size, and shape
of macromolecules.
• Useful for separation
and/or purification of
mixture of proteins
• This was the original
mode of
electrophoresis.
• Separation is based upon
the molecular weight of
proteins.
• The most common
method for determining
MW of proteins
• Very useful for checking
purity of protein samples
Native PAGE SDS PAGE
30. Applications
Used for estimation of molecular weight of proteins
and nucleic acids.
Determination of subunit structure of proteins.
Purification of isolated proteins.
Monitoring changes of protein content in body
fluids.
Identifying disulfide bonds between protein
Quantifying proteins
Blotting applications
31. 31
STARCH GEL ELECTROPHORESISSTARCH GEL ELECTROPHORESIS
A suspension of granular starch should be boiled in a buffer to give a clear colloidal
suspension.
The suspension on cooling sets as a semisolid gel due to intertwining of the branched
chains of amylopectin.
In order to avoid swelling and shrinking petroleum jelly is used.
ADVANTAGES:ADVANTAGES:
oHigh resolving power and sharp zones are obtained.
oThe components resolved can be recovered in reasonable yield especially proteins.
oCan be used for analytical as well as preparative electrophoresis.
DISADVANTAGES:DISADVANTAGES:
oElectro osmotic effect.
oVariation in pore size from batch to batch.