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This document provides an overview of electrophoresis, a technique used to separate charged molecules using an electric field. It defines electrophoresis as the migration of charged molecules under an external electric field. The document then discusses the principle, theory, factors affecting migration, and main types of electrophoresis - including moving boundary electrophoresis, zone electrophoresis using paper, gels, capillaries, and isotachophoresis and isoelectric focusing which separate molecules based on their electric charge and isoelectric point.
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Capillary electrophoresis is a separation technique that uses charged molecules' differential migration in response to an applied electric field. Key components include a capillary, buffers, and detectors. Molecules are separated based on their charge and size. There are several modes, including capillary zone electrophoresis which separates based on charge and size, and micellar electrokinetic capillary chromatography which uses micelles to separate charged and neutral molecules. Capillary electrophoresis provides high resolution, efficiency, and versatility in analyzing various molecules like proteins, nucleic acids, and inorganic ions.
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The phenomenon of electrophoresis was first observed by Russian professors Peter Ivanovich Strakhov and Ferdinand Frederic Reuss in 1807 at Moscow University. A constant application of electric field caused the particles of clay dispersed in water to migrate, showing an electrokinetic phenomenon.
Electrophoresis can be defined as an electrokinetic process that separates charged particles in a fluid using an electrical field of charge. Electrophoresis of cations or positively charged ions is sometimes referred to as cataphoresis (or cataphoretic electrophoresis). In contrast, sometimes, the electrophoresis of anions or negatively charged ions is referred to as anaphoresis (or anaphoric electrophoresis).
It’s used in a variety of applications. Though it is most often used in life sciences to separate protein molecules or DNA, it can be achieved through several different techniques and methods depending upon the type and size of the molecules.
The methods differ in some ways, but all we need is a source for the electrical charge, a support medium and a buffer solution. Electrophoresis is also used in laboratories for the separation of molecules based on their size, density and purity.
The method used to separate macromolecules such as DNA, RNA, or protein molecules is known as gel electrophoresis.
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Nucleic acid molecule sizing
DNA fragmentation for southern blotting
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The phenomenon of electrophoresis was first observed by Russian professors Peter Ivanovich Strakhov and Ferdinand Frederic Reuss in 1807 at Moscow University. A constant application of electric field caused the particles of clay dispersed in water to migrate, showing an electrokinetic phenomenon.
Electrophoresis can be defined as an electrokinetic process that separates charged particles in a fluid using an electrical field of charge. Electrophoresis of cations or positively charged ions is sometimes referred to as cataphoresis (or cataphoretic electrophoresis). In contrast, sometimes, the electrophoresis of anions or negatively charged ions is referred to as anaphoresis (or anaphoric electrophoresis).
It’s used in a variety of applications. Though it is most often used in life sciences to separate protein molecules or DNA, it can be achieved through several different techniques and methods depending upon the type and size of the molecules.
The methods differ in some ways, but all we need is a source for the electrical charge, a support medium and a buffer solution. Electrophoresis is also used in laboratories for the separation of molecules based on their size, density and purity.
The method used to separate macromolecules such as DNA, RNA, or protein molecules is known as gel electrophoresis.
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Nucleic acid molecule sizing
DNA fragmentation for southern blotting
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Protein fragmentation for western blotting
Separation of PCR products analysis
Detection and analysis of variations or mutations in the sequence
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Serum protein electrophoresis
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The fundamental principle of electrophoresis is the existence of charge separation between the surface of a particle and the fluid immediately surrounding it. An applied electric field acts on the resulting charge density, causing the particle to migrate and the fluid around the particle to flow.
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2. Both techniques provide information about the number and types of nuclei in different chemical environments within a molecule. However, 13C NMR is less sensitive than 1H NMR due to the lower gyromagnetic ratio and natural abundance of 13C.
3. 13C NMR spectra can show coupling between 13C-1H nuclei, but 13C-13C coupling is rarely observed due to the low abundance of 13C. Fourier transform techniques must be used for 13C NMR due to its low sensitivity.
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Mass spectroscopy is a technique used to analyze molecules. It involves ionizing molecules using electrons, accelerating the ions, and separating them based on their mass-to-charge ratio using electric or magnetic fields. The ions are then detected, producing a mass spectrum that is unique to each molecule and can be used to determine molecular structure. Mass spectroscopy requires only a small amount of sample and provides accurate molecular mass and elemental composition information. It is a destructive technique as the sample is consumed during ionization and fragmentation processes.
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The Nuclear Overhauser Effect (NOE) describes a change in the NMR signal intensity of one nuclear spin when a nearby spin is saturated. There are two main relaxation mechanisms, W0 and W2, that determine whether the NOE will be positive or negative. W0 typically leads to a negative NOE for macromolecules or in viscous solutions, while W2 usually gives a positive NOE for small molecules in non-viscous solutions. The magnitude of the NOE depends on factors like molecular weight, temperature, and solvent and can provide information about internuclear distances that is useful for assigning protein NMR spectra.
Isotachophoresis & ief(iso electric focusing
Isotachophoresis (ITP) and isoelectric focusing (IEF) are electrophoretic techniques used to separate ionic analytes. ITP separates analytes based on differences in ionic mobility in a discontinuous electrolyte system, resulting in sharpened zones. IEF separates molecules like proteins based on differences in their isoelectric point (pI) by exploiting the fact that a molecule's overall charge is dependent on the pH of its surroundings. Both techniques are useful for applications like protein analysis, metabolite analysis, and environmental analysis.
Transport number
This document discusses methods for determining transport numbers during electrolysis. It describes Hittorf's method and the moving boundary method. Hittorf's method involves electrolysis in a two-limbed vessel and analyzing changes in electrolyte concentration. The fraction of total current carried by each ion is equal to its transport number. The moving boundary method directly observes ion migration using a conductivity cell containing two solutions that form a boundary. Application of a current causes the boundary to move as ions migrate.
Equipments used in dispersed systems
This document discusses various types of equipment used to disperse systems. It describes mixers like propeller, turbine, anchor, and scraped surface agitators. It also discusses high speed dispersers, rotor-stator mixers, combination mixers, in-line mixers, and non-mechanical methods. Fine particle size reduction equipment like triple roll mills, ball mills, and bead mills are also covered. The document provides details on the working, applications, advantages and limitations of each type of dispersion equipment.
Paper electrophoresis
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.
solid dispersion
The document discusses solid dispersion and complexation techniques for improving the solubility and bioavailability of poorly soluble drugs. Solid dispersion involves combining a drug with a hydrophilic carrier to improve its dissolution rate. Types of solid dispersions include solid solutions, eutectic mixtures, and glass suspensions. Preparation techniques include hot melt, solvent evaporation, melt extrusion, and kneading. Complexation, such as drug-cyclodextrin inclusion complexes, enhances drug solubility and stability. These techniques are important for formulating oral drugs that are limited by poor solubility.
Water treatment process by RO UF
This document discusses various water treatment processes used in the pharmaceutical industry, including reverse osmosis (RO), demineralization (DM), and ultrafiltration. RO uses semipermeable membranes to remove dissolved solids, organic pyrogens, and microbes from water. DM removes mineral salts using ion exchange resins. Ultrafiltration uses membranes to retain suspended solids and high molecular weight substances while allowing water and low molecular solutes to pass through. The document also describes different types of treated pharmaceutical water like water for injection and their uses.
Air handling systems new
HVAC systems are an integral part of environmental control and include air handling units. AHU are large metal boxes that condition and circulate air, containing components like blowers, filters, and controls for temperature and humidity. Proper filtration is important for pharmaceutical facilities, utilizing filters like HEPA that can remove 99.97% of particles over 0.3 microns through mechanisms like impingement, diffusion, and interception. Dust collectors are also used to control air pollution and maintain clean environments through various collection methods. Regular inspection and maintenance of air handling systems is crucial to ensure quality pharmaceutical production.
Vaccines and sera
This document discusses vaccines and immunization. It defines active and passive immunization. Active immunization stimulates the immune system to produce antibodies to protect against disease, while passive immunization involves administering pre-formed antibodies to provide immediate, short-term protection. The document describes different types of vaccines, including live attenuated, inactivated, subunit, and combination vaccines. It also discusses sources of passive immunity like immune globulins and antisera from different species. Hypersensitivity reactions to foreign sera like anaphylaxis and serum sickness are mentioned.
Novel drug delivery systems
Dr. Maulik Patel's research focuses on developing new drug delivery systems to more selectively target drugs to the site of action. His goals are to increase bioavailability, provide controlled delivery, transport drugs intact to the target site while avoiding healthy tissue, and ensure stable delivery under physiological conditions. He examines various polymer-based formulations, micelles, liposomes, and nanotechnology approaches to better control drug release kinetics and targeting.
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Electrophoretic techniques for life science researchers
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Group 4 Analytical Chemistry-1.pptx
1. Electrophoresis is the migration of charged particles through a conductive medium such as a gel under the influence of an electric field. It is used to separate biomolecules like proteins and DNA based on their size and charge.
2. An electrophoretic system consists of two electrodes (anode and cathode) connected by an electrolyte medium. Charged particles migrate at different velocities depending on their size, shape, and charge, allowing for separation.
3. Factors like pH, ionic strength, voltage, and temperature influence electrophoretic separation. Applications include DNA analysis, antibiotic and vaccine testing, and studying protein-antibody interactions.
Electrophoresis
Electrophoresis is a physical method used to separate charged particles like proteins and amino acids using an electric field. It works by applying a voltage across a medium like paper or gel containing the sample, causing charged molecules to migrate at different rates depending on factors like their size, shape, and charge. The history of electrophoresis began in 1931 with Arne Tiselius' work separating proteins. It continues to be developed today and has applications in biochemistry like separating amino acids, proteins, enzymes, and antibiotics.
2103313001_dhavalkumar H rathod_MPH101T.pptx
The document discusses moving boundary electrophoresis and isoelectric focusing. It begins with an introduction to electrophoresis, defines key terms, and describes the principles and factors that affect electrophoresis. It then explains moving boundary electrophoresis, which separates molecules in solution without a supporting medium, and isoelectric focusing, which establishes a pH gradient to separate proteins by their isoelectric points. The document concludes by discussing applications and disadvantages of these techniques.
1 electrophoresis 1.pptx
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids. It works by applying an electric field to migrate molecules through a buffer solution or gel based on their size and charge. Key factors that affect migration rate are the net charge and size of the molecule, as well as the strength of the electric field and properties of the supporting medium used. Common electrophoresis methods include zone electrophoresis which uses a stabilizing gel matrix, and capillary electrophoresis where molecules are separated inside a thin capillary. The buffer system is also important as it carries current and determines the pH and charge of molecules during separation.
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This document provides an overview of electrophoresis and capillary electrophoresis. It defines electrophoresis as the differential movement of ions under an electric field based on their charge and size. Capillary electrophoresis separates ions in a capillary based on their electrophoretic mobility under an applied voltage. It discusses the principles, instrumentation, sample injection methods, detection methods, modes, and applications of capillary electrophoresis including genetic analysis, pharmaceutical analysis, and enantiomer separation.
Electrophoresis
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids. It works by applying an electric field to move molecules through a gel or other medium based on their size and charge. The document discusses the principles of electrophoresis, factors that affect separation like buffer composition and pH, and different electrophoresis techniques including paper, agarose gel, and polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis (PAGE) is commonly used to separate proteins based on their size and charge to mass ratio.
isoelectric focusing and Isotachophoresis.pptx
Capillary electrophoresis is a separation technique that uses thin capillaries to separate minute quantities of substances in a short time period with high resolution. Capillaries are typically 50 micrometers in diameter and 0.5-1 meter in length. Common modes of capillary electrophoresis include capillary zone electrophoresis, capillary gel electrophoresis, capillary electrochromatography, capillary isoelectric focusing, and capillary isotachophoresis. Isoelectric focusing separates proteins according to their isolectric points using a pH gradient gel, while capillary isotachophoresis migrates ions between a leading and terminating electrolyte at the same speed.
Electrophoresis
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
Electrophoresis
Electrophoresis is a technique used to separate charged particles such as proteins, nucleic acids, and other macromolecules. It works by applying an electric field to move these particles through a medium such as a gel or paper based on their size and charge. There are different types of electrophoresis including gel electrophoresis, paper electrophoresis, capillary electrophoresis, and isoelectric focusing which separates particles based on their isoelectric point. Electrophoresis has many applications in fields like forensics, molecular biology, genetics, and biochemistry to analyze proteins, DNA, RNA, and other biomolecules.
Electrophoresis
This document discusses electrophoresis, including:
- Its history beginning with Arne Tiselius developing moving boundary electrophoresis in the 1930s.
- The principle that charged particles migrate toward the cathode or anode depending on their charge when subjected to an electric field.
- Common supporting media like filter paper, cellulose acetate, agarose, and polyacrylamide gels that stabilize the medium and improve separation.
- Key factors that affect electrophoretic separation like pH, electric field strength, and properties of the supporting medium.
Other electrophoresis
It contains 2-3 acetyl groups per glucose unit and its adsorption capacity is less than that of paper.
It gives sharper bands.
Provides a good background for staining glycoproteins.
ADVANTAGE:
No tailing of proteins or hydrophilic materials.
Available in wide range of particle size and layer thickness.
Give sharp bands and offer good resolution.
High voltage can be applied which will enhance the resolution.
Modern pharmaceutical analytical technique ( Electrophoresis)
This document provides an overview of electrophoresis, including definitions, principles, types, and applications. It discusses four main types of electrophoresis: paper electrophoresis, gel electrophoresis, capillary electrophoresis, and iso-electric electrophoresis. Paper and gel electrophoresis are described as zone electrophoresis techniques that separate components into bands on a supporting medium like paper or gel. Capillary electrophoresis allows separation in free solution within a thin capillary tube. Iso-electric electrophoresis separates molecules based on their iso-electric point, the pH where they have no net charge. The document outlines the principles, instrumentation, and applications of each electrophoresis technique.
electrophorosis (1).pptx
This presentation discusses various types of electrophoresis, including paper electrophoresis, gel electrophoresis, capillary electrophoresis, and moving boundary electrophoresis. It explains the basic principles of electrophoresis, which involves the separation of charged particles in a conducting medium under the influence of an electric field. Factors that affect electrophoresis like charge, size, and pH are also summarized. The instrumentation and applications of each type of electrophoresis are briefly described.
Electrophorsis PRINCIPLE ,INSTRUMENTATION & FACTOR AFFECTING WITH APPLICATION...
This document discusses electrophoresis, which is a technique where charged molecules like proteins and nucleic acids migrate in an electrical field. The rate of migration depends on factors like the molecule's charge, size, shape, and the buffer properties. Electrophoresis is usually done with gels placed between two buffer chambers with electrodes. The key factors affecting electrophoresis are the sample properties, electric field strength, buffer composition and properties, and the supporting medium. Electrophoresis has applications in diagnostic testing and analyzing biological molecules like proteins.
Electrophoresis
This document provides an overview of electrophoresis. It defines electrophoresis as the migration of electrically charged particles or ions in solutions due to an applied electric field. It describes the basic theory behind electrophoresis, including how electrophoretic mobility determines the speed at which ions or solutes move. It also outlines the key components of an electrophoresis apparatus and describes the basic procedure for performing electrophoresis, including sample preparation, gel preparation, running the electrophoresis, and visualizing the results. Finally, it discusses several applications of electrophoresis across various fields like forensics, molecular biology, genetics, microbiology, and biochemistry.
Electrophoresis
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids. It works by applying an electric field to move molecules through a buffer solution or gel based on their size and charge. There are several types of electrophoresis that use different supporting media like agarose gel, polyacrylamide gel, cellulose acetate, or paper to separate molecules. Factors like pH, buffer composition, strength of electric field, and temperature influence how molecules separate during electrophoresis. It has various applications in biomedical research and clinical diagnostics.
4. Electrophoresis.pptx
Electrophoresis is a technique used to separate charged molecules like proteins based on their size and charge. It involves placing samples containing these molecules in an electric field, which causes them to migrate at different rates towards the positive or negative electrode depending on their charge. There are several types of electrophoresis that differ in the medium used to separate the molecules, such as paper, agarose gel, and polyacrylamide gel electrophoresis. Factors like the molecule's charge, size, shape, and the buffer properties determine how fast it will migrate. Interpretation involves visualizing bands that form on the medium after staining to analyze the separated components.
Dep
This document describes an experiment to study how yeast cells move when subjected to non-uniform electric fields (dielectrophoresis). Yeast cells were placed in a suspension between two pointed platinum electrode tips and exposed to alternating electric fields of varying frequency. The motion and clustering of cells at the electrode tips, where the electric field was strongest, was observed under a microscope over time. The clustering behavior depended on factors like field strength, frequency, suspension conductivity, and biological characteristics of the yeast cells.
ELECTROPHORESIS.pptx
This document provides an overview of electrophoresis, including its principle, working conditions, factors affecting separation, and types. Electrophoresis is an analytical technique that separates charged molecules like proteins and nucleic acids based on their movement in an electric field. It works by applying a voltage to move molecules through a buffer solution or gel support medium. The rate of migration depends on factors like the molecule's charge, size, and the electric field strength. Common electrophoresis techniques described include zone electrophoresis using paper, gels, and thin layers, as well as moving boundary methods like capillary electrophoresis.
paper ELECTROPHORIS.pptx
Paper electrophoresis is a technique used to separate charged biomolecules like proteins and nucleic acids. It works by applying an electric field to a strip of filter paper soaked in buffer solution. The charged molecules migrate along the paper at different rates depending on their size and charge, separating into distinct bands. Key factors that affect separation are the properties of the sample molecules, the electric field strength and voltage gradient, the buffer composition and pH, and interactions with the paper medium. Paper electrophoresis has applications in clinical testing, forensic analysis, and environmental monitoring.
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Modern pharmaceutical analytical technique ( Electrophoresis)
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Dev
- 1. EVALUATION SEMINAR SUBJECT: MODERN PHARMACEUTICAL ANALYSIS TOPIC: ELECTROPHORESIS Presented by DEVI. S I M. Pharm, Department of Pharmaceutics, M.S.R.C.P, Bangalore-54.
- 2. CONTENTS ¤ Introduction ¤ Definition and Principle ¤ Theory ¤ Factors affecting the migration of ions ¤ Types of electrophoresis o Moving boundary electrophoresis o Zone electrophoresis
- 3. INTRODUCTION Electrophoresis is a physical method of analysis which involves separation of the compounds that are capable of acquiring electric charge in conducting electrodes. ELECTROPHORESIS (Greek word)=BORNE BY ELECTRICITY It is a separation technique in which the components are separated due to their varying behavior under the influence of an applied electric field. The technique was pioneered in 1937 by the Swedish chemist Arne Tiselius for the separation of proteins.
- 4. DEFINITION AND PRINCIPLE Electrophoresis is defined as the “migration of charged molecules under the influence of an external electric field” In practical terms, a positive (anode) and negative (cathode) electrode are placed in a solution containing ions. Then, when a voltage is applied across the electrodes, solute ions of different charge, i.e., anions (negative) and cations (positive), will move through the solution towards the electrode of opposite charge.
- 5. THEORY Ion migration velocity can be expressed as: V=µeE The applied field (Fef) (driving force) : Fef=qE The friction (Ffr) drag is given by: Ffr=6ήπrv At equilibrium: Fef=Ffr Therefore: qE=6ήπrv
- 6. FACTORS AFFECTING THE MIGRATION OF IONS Factors related to the sample Charge Size Shape Properties of electric field Potential difference Current Resistance Environmental characteristics pH Temperature Electrolyte concentration Composition and nature of supporting medium Buffer Supporting medium
- 7. TYPES OF ELECTROPHORESIS Free solution / frontal / moving boundary electrophoresis: supporting medium is absent Zone electrophoresis: supporting medium is present 1) Paper electrophoresis 2) Gel electrophoresis 3) Capillary electrophoresis 4) Continuous electrophoresis 5) Isotachophoresis 6) Iso electric focusing
- 9. ZONE ELECTROPHORESIS Paper electrophoresis a) Open strip Paper Electrophoresis Horizontal Vertical b) Closed strip Paper Electrophoresis Horizontal Vertical
- 10. c. Immersed strip Paper Electrophoresis - + Cooling liquid Filter paper Buffer d. Enclosed strip Paper Electrophoresis
- 14. ISOTACHOPHORESIS Iso-equal , tachos- speed, phoresis-migration The technique of Isotachophoresis depends on the development of potential gradient. Principle: A leading electrolyte(chloride) with a higher mobility than the analytes and a trailing electrolyte(glycinate) with a lower mobility are used. After application of an electric potential a low electrical field is created in the leading electrolyte and a high electrical field in the terminating electrolyte. The pH at sample level is determined by the counter-ion of the leading electrolyte that migrates in the opposite direction.
- 16. ISO ELECTRIC FOCUSINNG(IEF) » Proteins carry both positive and negative charges, which is the PH when molecule has no net charge. » The pH which gives zero net charge is the isoelectric point or pH. » Generally proteins readily crystallize at the isoelectric point. » Most of the proteins have isoelectric point of 5-9. » When electrophoresis is run in a solution buffered at constant PH , proteins having a net charge will migrate towards the opposite electrode so long as the current flows. » The use of PH gradient across the supporting medium causes each protein to migrate to an area of specific PH » Proteins are found at the point of the gradient where they carry no net charge. » The PH of the protein equals the PH of the gradient, thus resulting in sharp well defined protein bands.
- 17. REFERENCES 1. Instrumental methods of chemical analysis by B.K. sharma pg.no C269-c281. 2. Electrophoresis by Melvin wiley publications. 3. http://en.wikipedia.org/wiki/Electrophoresis. 4. www.pharmainfo.net. 5. Theory of Electrophoresis-K.S. Pitre, Dr. Harisingh Gour University, Sagar, India, Encyclopedia of Analytical Science. 6. http://books.google.co.in 7. Fundamentals of Analytical chemistry-Skoog (pg.no-1003)
- 20. ‘winning doesn’t always mean being first, means ur doing better than you have done before’ Bonnie Blair