The Protein Protocols Handbook
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| Other Authors: | |
| Summary: | LXX, 1984 p. text |
| Language: | English |
| Published: |
Totowa, NJ :
Humana Press : Imprint: Humana,
2009.
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| Edition: | 3rd ed. 2009. |
| Series: | Springer Protocols Handbooks,
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| 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.