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  • Produktbild: Methods of Protein and Nucleic Acid Research
  • Produktbild: Methods of Protein and Nucleic Acid Research

Methods of Protein and Nucleic Acid Research Volume 1: Electrophoresis · Isoelectric Focusing Ultracentrifugation

Fr. 137.00

inkl. gesetzl. MwSt., Versandkostenfrei

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

13.04.2012

Verlag

Springer Berlin

Seitenzahl

344

Maße (L/B/H)

24.4/17/2 cm

Gewicht

614 g

Auflage

Softcover reprint of the original 1st ed. 1984

Sprache

Englisch

ISBN

978-3-642-87487-1

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

13.04.2012

Verlag

Springer Berlin

Seitenzahl

344

Maße (L/B/H)

24.4/17/2 cm

Gewicht

614 g

Auflage

Softcover reprint of the original 1st ed. 1984

Sprache

Englisch

ISBN

978-3-642-87487-1

Herstelleradresse

Springer-Verlag GmbH
Tiergartenstr. 17
69121 Heidelberg
DE

Email: GPSR Kontakt

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  • Produktbild: Methods of Protein and Nucleic Acid Research
  • Produktbild: Methods of Protein and Nucleic Acid Research
  • I Electrophoresis.- 1 Gels for Electrophoresis.- 1.1 Polyacrylamide Gel (PAAG).- 1.1.1 Reagents.- 1.1.2 Polymerization Process.- 1.1.3 Selection of Concentration of Monomers.- 1.2 Agarose.- 1.3 Mixed Gels (Agarose + PAAG).- 1.4 Cellulose Acetate Strips Impregnated with PAAG.- 2 Techniques of Gel Preparation and Necessary Equipment.- 2.1 Vertical Tube Electrophoresis.- 2.2 Vertical Slab Electrophoresis.- 2.3 Horizontal Slab Electrophoresis.- 3 Electrophoresis of Proteins.- 3.1 General Remarks.- 3.1.1 Migration of Proteins in Gels.- 3.1.2 Electric Field Strength.- 3.1.3 Choice of Running Gel Buffer.- 3.1.4 Heat Evolution During Electrophoresis.- 3.1.5 Gel Loading: Width of Protein Bands.- 3.1.6 Introduction of Urea and ?-Mercaptoethanol. Possible Artifacts.- 3.1.7 Tracking Dyes.- 3.1.8 Separation of Proteins According to Size and Charge.- 3.1.9 Choice of Running Buffer.- 3.1.10 Use of Urea.- 3.1.11 Gel Loading and Sample Preparation.- 3.1.12 Selected Examples.- 3.2 Separation of Proteins on the Basis of Size in the Presence of Sodium Dodecyl Sulphate (SDS).- 3.2.1 Principles of the Method.- 3.2.2 Selection of Gel Porosity.- 3.2.3 Influence of Urea and Nonionic Detergents.- 3.2.4 Selection of Running Buffer.- 3.2.5 Preparation of Protein Samples.- 3.2.6 Electrophoresis.- 3.2.7 Staining and Elution of Proteins.- 3.3 Disc Electrophoresis.- 3.4 Pore Gradient PAAG.- 3.5 Two-Dimensional PAAG-Electrophoresis.- 3.6 Electrophoresis in the Presence of Triton X-100 and Cetavlon.- 3.6.1 Triton X-100.- 3.6.2 Cetavlon.- 3.6.3 Affinity Electrophoresis.- 3.7 Staining of Proteins in PAAG.- 3.7.1 Acidic Dyes.- 3.7.2 Other Dyes and Methods of Staining.- 3.7.3 Fluorescent Dyes.- 3.7.4 Detection of Enzymes After Electrophoresis.- 3.7.5 Detection of Protein Bands by Precipitation of SDS.- 3.8 Elution of Proteins from the Gel.- 3.9 Determination of Protein Radioactivity After PAGE.- 3.9.1 Counting of Protein Eluates.- 3.9.2 Solubilization of PAAG.- 3.9.3 Gels Impregnated with Scintillant.- 3.9.4 Autoradiography.- 3.9.5 Fluorography.- 3.10 Preparative Electrophoresis of Proteins.- 4 Electrophoresis of Nucleic Acids.- 4.1 General Remarks.- 4.1.1 Choice of Buffer and Electric Field Strength.- 4.1.2 Choice of Character and Porosity of Gel.- 4.1.3 Influence of Secondary Structure of Nucleic Acids.- 4.1.4 Marker Molecules.- 4.1.5 Tracking Dyes.- 4.2 Electrophoresis Under Mild Conditions.- 4.2.1 Fractionation of Plasmids and DNA Fragments.- 4.2.2 Fractionation of RNA.- 4.3 Electrophoresis in Denaturating Gels.- 4.3.1 Alkaline Gels.- 4.3.2 Urea-containing Gels. Sequencing of DNA and RNA.- 4.3.3 Denaturating Gels Containing Formamide.- 4.3.4 Denaturating Gels Containing Formaldehyde.- 4.3.5 Gels Containing Methylmercury Hydroxide.- 4.3.6 Denaturation of Nucleic Acids with Glyoxal.- 4.4 Application of Pore Gradient PAAG.- 4.5 Two-Dimensional Electrophoresis of Nucleic Acids and Their Fragments.- 4.6 Specific Examples of Electrophoresis of Nucleic Acids.- 4.6.1 Electrophoresis of the Ternary Complex of DNA-RNA-polymerase-RNA in Agarose Gel.- 4.6.2 Detection of mRNA After Agarose-Gel Electrophoresis of Total RNA.- 4.6.3 The Use of Liquid (Non-Cross-Linked) PAAG.- 4.6.4 Separation of Okazaki Fragments from a Total Cell Lysate.- 4.7 Staining of Nucleic Acids After Electrophoresis.- 4.8 Elution of Nucleic Acids from Gels.- 4.8.1 Elution from PAAG Due to Diffusion.- 4.8.2 Elution from Agarose Gels.- 4.8.3 Electrophoretic Elution.- 4.8.4 Transfer of Nucleic Acids from Gels onto Nitrocellulose Filters and Diazopaper.- 4.9 Determination of Radioactivity.- 4.10 Preparative Electrophoresis of Nucleic Acids.- II Isoelectric Focusing (IEF).- 1 Principle of the Method.- 1.1 Migration of Proteins in a pH Gradient.- 1.2 Ampholytes for IEF.- 1.3 Generation of a pH Gradient.- 1.4 Electrical Conductivity Problem.- 1.5 Comparison of Properties of Commercial Ampholytes.- 1.6 Danger of Appearance of a Zone of Pure Water.- 1.7 Resolving Power. Choice of pH Interval.- 1.8 Physicochemical Characteristics of Ampholytes.- 1.9 Endosmosis.- 1.10 Immobilized pH Gradients.- 2 Analytical Variations of IEF.- 2.1 IEF in Horizontal Slabs of PAAG.- 2.2 Preparation of PAAG for IEF.- 2.3 Use of Urea and Detergents.- 2.4 Preparation of Slabs and Apparatus.- 2.5 Sample Application.- 2.6 Operating Conditions and Duration of IEF.- 2.7 Measurement of pH.- 2.8 Staining of Protein Zones.- 2.8.1 Two-Step Staining.- 2.8.2 Enzymatic Reactions.- 2.9 IEF in Tubes of PAAG.- 2.10 IEF in Horizontal Slabs of Agarose.- 3 Two-Dimensional Fractionation of Proteins.- 3.1 Method of O’Farrell.- 3.2 Modifications of the Method of O’Farrell.- 3.3 Sparingly Soluble Membrane Proteins.- 3.4 Electrophoresis Together with the pH Gradient Generation.- 3.5 Interpretation of Two-Dimensional Fractionation Patterns of Proteins According to O’Farrell.- 3.6 The Use of IEF for the Second-Dimension Run.- 3.7 Electrophoresis of Proteins Across the pH Gradient.- 4 Preparative Variants of IEF.- 4.1 IEF in a Layer of Granulated Gel.- 4.1.1 Preparation of the Gel Bed.- 4.1.2 Sample Application.- 4.1.3 Conditions of IEF.- 4.1.4 Detection and Elution of Proteins.- 4.2 IEF in Sucrose Density Gradients.- 4.2.1 Design of the Column.- 4.2.2 Filling of the Column.- 4.2.3 Sample Application.- 4.2.4 Operating Conditions of IEF.- 4.2.5 Unloading of the Column.- 4.2.6 Specific Problems.- 4.2.7 Choice of Electrode Polarity.- 4.2.8 Danger of Precipitation.- 4.2.9 Solubility Problems.- 4.2.10 Maximum Loading.- 4.2.11 Fractionation of Ampholytes into Narrow pH Intervals.- 4.2.12 The ISCO Columns.- 5 Isotachophoresis.- III Ultracentrifugation.- 1 Sedimentation — Basic Concepts.- 1.1 Buoyant Density of Particles.- 2 Ultracentrifuge.- 2.1 Principles of Action and Arrangement of Main Units.- 2.2 Points to be Checked by Experimenter.- 2.3 Making a Run.- 3 Rotors and Tubes.- 3.1 Fixed Angle Rotors.- 3.1.1 Tubes for Fixed Angle Rotors.- 3.1.2 Care of Rotors and Tubes.- 3.2 Swinging Bucket Rotors.- 3.3 Vertical Tube Rotors.- 3.4 Maximum Speed of Rotation.- 3.5 Zonal Rotors.- 3.5.1 Specific Requirements in the Exploitation and Care of Zonal Rotors.- 4 Differential Centrifugation (Pelleting).- 5 Rate-Zonal Centrifugation.- 5.1 Sedimentation Constant.- 5.2 Isokinetic Density Gradient.- 5.3 Choice of Medium for Rate-Zonal Centrifugation.- 5.4 Properties of Sucrose Solutions.- 5.5 The Shape of the Sucrose Gradient.- 5.6 Preparing and Unloading Sucrose Gradients.- 5.6.1 Loading of the Sample onto a Gradient.- 5.6.2 Fractionation of the Gradient.- 5.6.3 Analysis of Gradients.- 5.7 Choice of Operating Conditions.- 5.8 Examples of Centrifugation in Sucrose Gradients.- 5.8.1 Fractionation of Ribonucleoproteins.- 5.8.2 Fractionation of RNA.- 5.8.3 Fractionation of DNA.- 6 Equilibrium (Isopycnic) Centrifugation.- 6.1 Modes of Preparation and General Characterization of Density Gradients.- 6.2 Choice of Salt for Preparation of Density Gradients.- 6.3 Density Gradients of CsCl Solutions.- 6.3.1 Preformed Gradients.- 6.3.2 Equilibrium Centrifugation in Fixed Angle Rotors.- 6.3.3 Centrifugation in Vertical Tube Rotors.- 6.3.4 Unloading and Monitoring of Isopycnic Gradients.- 6.3.5 Examples of Equilibrium Centrifugation in Density Gradients of CsCl.- 6.4 Cs2SO4 Density Gradients.- 6.5 Caesium and Rubidium Trichloroacetate Density Gradients.- 6.6 KI and NaI Density Gradients.- 6.7 Metrizamide Density Gradients.- 7 Centrifugation in Zonal Rotors.- References to Part I.- References to Part II.- References to Part III.- List of Selected Examples.- Nomograms for Calculation of Centrifugation Time (for Practical Use).