The Protein Protocols Handbook

Bibliographic Details
Corporate Author: SpringerLink (Online service)
Other Authors: Walker, John M. (Editor)
Summary:LXX, 1984 p.
text
Language:English
Published: Totowa, NJ : Humana Press : Imprint: Humana, 2009.
Edition:3rd ed. 2009.
Series:Springer Protocols Handbooks,
Subjects:
Online Access:https://doi.org/10.1007/978-1-59745-198-7
Format: Electronic Book
Table of Contents:
  • Protein Determination by UV Absorption
  • The Lowry Method for Protein Quantitation
  • The Bicinchoninic Acid (BCA) Assay for Protein Quantitation
  • The Bradford Method for Protein Quantitation
  • Ultrafast Protein Determinations Using Microwave Enhancement
  • The Nitric Acid Methods for Protein Estimation in Biological Samples
  • Quantitation of Tryptophan in Proteins
  • Kinetic Silver Staining of Proteins
  • Quantitation of cellular proteins by flow cytometry
  • Quantitation of cellular proteins by laser scanning cytometry
  • Protein Solubility in 2D Electrophoresis: Basic principles and issues
  • Mouse and Human Tissues Sample Preparation for 2-D Electrophoresis
  • Plant Protein sample preparation for 2DE
  • Preparation of bacterial samples for 2-D PAGE
  • Preparation of bodily fluids for 2-D PAGE
  • Immunoaffinity Depletion of high abundance plasma and serum proteins
  • Preparation of Yeast samples for 2D PAGE
  • Membrane Protein Preparation Using Aqueous Polymer Two Phase Systems
  • Subcellular fractionation of small sample amounts
  • Nondenaturing Polyacrylamide Gel Electrophoresis of Proteins
  • SDS Polyacrylamide Gel Electrophoresis of Proteins
  • Gradient SDS Polyacrylamide Gel Electrophoresis of Proteins
  • SDS-Polyacrylamide Gel Electrophoresis of Peptides
  • Blue native gel electrophoresis (BN-PAGE)
  • Separation of proteins by gel electrophoresis in the Tris-Taurine-HCl system
  • Cetyltrimethylammonium Bromide Discontinuous Gel Electrophoresis of Proteins: M -Based Separation of Proteins with Retained Native Activity
  • Acetic Acid-Urea Polyacrylamide Gel Electrophoresis of Basic Proteins
  • Acid-Urea-Triton Polyacrylamide Gel Electrophoresis of Histones
  • Isoelectric Focusing of Proteins in Ultra-Thin Polyacrylamide Gels
  • Serial immobilized pH gradient isoelectric focusing over pH 4-9
  • Radiolabelling of Eukaryotic Cells and Subsequent Preparation for 2-D
  • Two-Dimensional PAGE Using Carrier Ampholyte pH Gradients in the First Dimension
  • Vertical agarose electrophoresis and electroblotting of high molecular weight proteins
  • 2D PAGE of high molecular weight proteins
  • Casting immobilised pH gradients
  • Nonequilibrium pH Gel Electrophoresis
  • Microchip capillary electrophoresis
  • Protein Separations in Microfluidic Chips
  • Difference gel electrophoresis (DIGE)
  • Comparing 2-D Electrophoresis Gels Across Internet Databases
  • Quantification of Radiolabeled Proteins in Polyacrylamide Gels 25.4.07
  • Differential ProteoTope radioactive quantification of protein abundance ratios
  • Quantitation of Proteins on Polyacrylamide Gels
  • Using SDS-PAGE and scanning laser densitometry to measure proteins
  • Rapid and Sensitive Staining of Unfixed Proteins in Polyacrylamide Gels with Nile Red
  • Zinc reverse staining technique
  • Protein Staining with Calconcarboxylic Acid in Polyacrylamide Gels
  • Detection of Proteins in Polyacrylamide Gels by Silver Staining
  • Background-free Protein Detection on Polyacrylamide Gels and on Electroblots Using Transition Metal Chelate Stains
  • Detection of Proteins in Polyacrylamide Gels by Fluorescent Staining
  • Detection of Glycoproteins in Gels and Blots
  • Staining of Glycoproteins/Proteoglycans on SDS-Gels
  • Detection of Proteins and Sialoglycoproteins in Polyacrylamide Gels Using Eosin X stain
  • Pro-Q Diamond phosphoprotein staining
  • Electroelution of Proteins from Polyacrylamide Gels
  • Autoradiography and Fluorography of Acrylamide Gels
  • Proteolytic Activity Detection by Two-Dimensional Zymography
  • Protein Blotting by Electroblotting
  • Protein Blotting by the Semi-dry Method
  • Protein Blotting by the Capillary Method
  • Western Blotting of basic proteins electrophoretically resolved on acid-urea-Triton-polyacrylamide gels
  • Immunoblotting of 2-DE Separated Proteins
  • High efficiency blotting of high-molecular weight proteins
  • Alkaline Phosphatase Labeling of IgG Antibody
  • b-Galactosidase Labeling of IgG Antibody
  • Horseradish Peroxidase Labeling of IgG Antibody
  • Digoxigenin (DIG) Labelling of IgG Antibody
  • Conjugation of fluorochromes to antibodies
  • Coupling of Antibodies with Biotin
  • Preparation of Avidin Conjugates
  • MDPF Staining of Proteins on Western Blots
  • Copper Iodided Staining of Proteins and its silver enhancement
  • Detection of Proteins on Blots using Direct Blue 71
  • Detection of proteins on Western blots using colorimetric and radiometric vusialization of Secondary Ligands
  • Identification of Glycoproteins on Nitrocellulose Membranes Using Lectin Blotting
  • A Sensitive Method to Quantitatively Detect Total Protein on Membranes after Electrophoretic Transfer Using Avidin- or Streptavidin-Biotin
  • Detection and Quantification of Proteins on Immunoblots using Enhanced Chemiluminescence
  • Reutilization of Western Blots After Chemiluminescent Detection or Autoradiography
  • The use of quantum dot luminescent probes for Western blot analysis
  • The use of infrared fluorescent dyes in quantitative immunoblotting
  • The use of infrared fluorescent dyes in immunofluorescence microscopy
  • Carboxymethylation of Cysteine Using Iodoacetamide/Iodoacetic Acid
  • Performic Acid Oxidation
  • Succinylation of Protein
  • Pyridylethylation of Cysteine Residues
  • Side-Chain Selective Chemical Modifications of Proteins
  • Nitration of Tyrosines
  • Ethoxyformylation of Histidine
  • Modification of Arginine Side Chains with p-Hydroxyphenylglyoxal
  • Amidination of Carboxyl Groups
  • Amidination of Lysine Side Chains
  • Modification of tryptophan with 2-Hydroxy-5-Nitrogenzylbromide
  • Modification of Sulhydryl Groups with DTNB
  • Chemical Cleavage of Proteins at Methionyl-X Peptide Bonds
  • Chemical Cleavage of Proteins at Tryptophanyl-X Peptide Bonds
  • Chemical Cleavage of Proteins at Aspartyl-X Peptide Bonds
  • Chemical Cleavage of Proteins at Cysteinyl-X Peptide Bonds
  • Chemical Cleavage of Proteins at Asparaginyl-Glycyl Peptide Bonds
  • Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels
  • On-PVDF protein digestions for N-terminal sequencing and peptide mass fingerprinting
  • Enzymatic Digestion of Proteins on PVDF membranes
  • Reverse Phase HPLC Separation of Enzymatic Digests of Proteins
  • Peptide Mapping by Two-Dimensional Thin-Layer Electrophoresis-Thin-Layer Chromatography
  • Peptide Mapping by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis
  • Peptide Mapping by High-Performance Liquid Chromatography
  • Production of Protein Hydrolysates Using Enzymes
  • Amino Acid Analysis by Precolumn Derivatization with 1- Fluoro-2,4-Dinitrophenyl-5-L-Alanine Amide (Marfey’s Reagent)
  • Amino acid analysis in protein hydrolysates using anion exchange chromatography and IPAD detection
  • Validation of amino acid analysis
  • Molecular Weight Estimation for Native Proteins Using High-Performance Size Exclusion Chromatography
  • Detection of Disulfide-Linked Peptides by HPLC
  • Detection of Disulfide-Linked Peptides by Mass Spectrometry
  • Diagonal Electrophoresis for Detecting Disulfide Bridges
  • Estimation of Disulfide Bonds Using Ellman’s Reagent
  • Quantitation of Cysteine Residues and Disulfide Bonds by Electrophoresis
  • N-Terminal sequencing of the N-terminally Modified Proteins
  • De-blocking of Proteins containing N-Terminal Pyroglutamic Acid
  • Detection and characterization of protein mutations by mass spectrometry
  • Peptide Sequencing by Nanoelectrospray Tandem Mass Spectrometry
  • Protein identification by Peptide mass fingerprinting using MALDI-TOFF Mass spectrometry
  • Protein ladder sequencing
  • Sequence Analysis with WinGene/WinPep
  • HPLC and MS of integral membrane proteins
  • Enrichment of Serum Peptides and Analysis by MALDI-TOF Mass Spectrometry
  • Computational Methods for the Analysis of MALDI-TOF Spectra to Discover Peptide Serum Biomarkers
  • Simple tools for complex N-glycan analysis
  • A Lectin-Binding Assay for the Rapid Characterization of the Glycosylation of Purified Gycoproteins
  • Chemical Methods of Analysis of Glycoproteins
  • Monosaccharide Analysis by HPAEC
  • Monosaccharide Analysis by GC
  • Determination ofmonosaccharide linkage and Substitution Patterns by GC.MS Methylation Analysis
  • Sialic Acid Analysis by HPAEC-PAD
  • Chemical Release of O-Linked Oligosaccharide Chains
  • O-Linked Oligosaccharide Profiling by HPLC
  • O-Linked Oligosaccharide Profiling by HPAEC-PAD
  • Release of N-Linked Oligosaccharide Chains by Hydrazinolysis
  • Enzymatic Release of O- and N-Linked Oligosaccharide Chains
  • N-Linked Oligosaccharide Profiling by HPLC on Porous Graphitized Carbon (PGC)
  • N-linked Oligosaccharide Profiling by HPAEC-PAD
  • HPAE-PAD analysis of monosaccharides released by exoglycosidase digestion
  • Microassay Analyses of Protein Glycosylation
  • Polyacrylamide gel electrophoresis of fluorophore-labeled carbohydrates from glycoproteins
  • HPLC Analysis of fluorescently labelled glycans
  • Glycoprofiling purified glycoproteins using Surface Plasmon Resonance
  • Sequencing Heparan Sulphate Saccharides
  • Analysis of glycoprotein heterogeneity by Capillary Electrophoresis and Mass Spectrometry
  • Affinity chromatography of oligosaccharides and glycopeptides with immobilized lectins
  • In-Gel Enzymatic Release of N-glycans
  • Analysis of N-Linked glycans by mass spectrometry
  • MS Analysis of Protein glycosylation
  • Mapping protein N-glycosylation by COFRADIC
  • Mass spectrometric analysis of O-linked glycans released directly from Glycoproteins in gels using ß-elimination
  • Glycopeptide analysis using LC/MS and LC/MSn
  • Identification of Vitamin K-Dependent Proteins Using a Gla-specific Monoclonal Antibody
  • The identification of protein S-Nitrocysteine
  • Detection of nitrotyrosine-containing proteins
  • Mass spectrometric determination of protein Ubiquitination
  • Detection of Sumoylated Proteins
  • Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography
  • Analyzing Protein Phospho.