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Preface | |
Contributors | |
Protein Determination by UV Absorption | p. 3 |
The Lowry Method for Protein Quantitation | p. 7 |
The Bicinchoninic Acid (BCA) Assay for Protein Quantitation | p. 11 |
The Bradford Method for Protein Quantitation | p. 15 |
Ultrafast Protein Determinations Using Microwave Enhancement | p. 21 |
Quantitation of Tryptophan in Proteins | p. 29 |
Protein Quantitation Using Flow Cytometry | p. 33 |
Copper Iodide Staining of Proteins on Solid Phases | p. 39 |
Kinetic Silver Staining of Proteins Adsorbed to Microtiter Plates | p. 45 |
Nondenaturing Polyacrylamide Gel Electrophoresis of Proteins | p. 51 |
SDS Polyacrylamide Gel Electrophoresis of Proteins | p. 55 |
Gradient SDS Polyacrylamide Gel Electrophoresis of Proteins | p. 63 |
Cetyltrimethylammonium Bromide Discontinuous Gel Electrophoresis of Proteins: M[subscript r]-Based Separation of Proteins with Retained Native Activity | p. 67 |
Acetic Acid-Urea Polyacrylamide Gel Electrophoresis of Basic Proteins | p. 83 |
Acid-Urea-Triton Polyacrylamide Gels for Histones | p. 91 |
SDS-Polyacrylamide Gel Electrophoresis of Peptides | p. 101 |
Isoelectric Focusing of Proteins in Ultra-Thin Polyacrylamide Gels | p. 109 |
Isoelectric Focusing Under Denaturing Conditions | p. 115 |
Radioisotopic Labeling of Proteins for Polyacrylamide Gel Electrophoresis | p. 121 |
Two-Dimensional PAGE Using Carrier Ampholyte pH Gradients in the First Dimension | p. 127 |
Two-Dimensional PAGE Using Immobilized pH Gradients | p. 133 |
Two-Dimensional PAGE Using Flat-Bed IEF in the First Dimension | p. 139 |
Free Zone Capillary Electrophoresis | p. 143 |
Capillary Isoelectric Focusing with Electro-Osmotic Flow Mobilization | p. 155 |
Quantification of Radiolabeled Proteins in Polyacrylamide Gels | p. 161 |
Quantification of Proteins by Staining in Polyacrylamide Gels | p. 167 |
Quantitation of Proteins Separated by Electrophoresis Using Coomassie Brilliant Blue | p. 173 |
Rapid Staining of Proteins in Polyacrylamide Gels with Nile Red | p. 179 |
Zn[superscript 2+]-Reverse Staining of Proteins in Polyacrylamide Gels | p. 187 |
Protein Staining with Calconcarboxylic Acid in Polyacrylamide Gels | p. 197 |
Detection of Proteins and Sialoglycoproteins in Polyacrylamide Gels Using Eosin Y Stain | p. 203 |
Electroelution of Proteins form Polyacrylamide Gels | p. 207 |
High-Performance Electrophoresis Chromatography | p. 215 |
Drying Polyacrylamide Gels | p. 223 |
Detection of Proteins in Polyacrylamide Gels by Silver Staining | p. 229 |
Autoradiography and Flourography of Acrylamide Gels | p. 235 |
Protein Blotting by Electroblotting | p. 245 |
Protein Blotting by the Semidry Method | p. 249 |
Protein Blotting by the Capillary Method | p. 261 |
Protein Blotting of Basic Proteins Resolved on Acid-Urea-Triton-Polyacrylamide Gels | p. 263 |
Alkaline Phosphatase Labeling of Antibody Using Glutaraldehyde | p. 269 |
[Beta]-Galactosidase Labeling of Antibody Using MBS | p. 271 |
Horseradish Peroxidase Labeling of Antibody Using Periodate Oxidation | p. 273 |
Protein Staining and Immunodetection Using Colloidal Gold | p. 275 |
Fluorescent Protein Staining on Nitrocellulose with Subsequent Immunodetection of Antigen | p. 289 |
Coupling of Antibodies with Biotin | p. 293 |
Preparation of Avidin Conjugates | p. 303 |
Detection of Polypeptides on Blots Using Secondary Antibodies or Protein A | p. 313 |
Detection of Proteins on Blots Using Avidin- or Streptavidin Biotin | p. 323 |
Detection of Proteins on Blots Using Chemiluminescent Systems | p. 329 |
Carboxymethylation of Cysteine Using Iodoacetamide/Iodoacetic Acid | p. 339 |
Performic Acid Oxidation | p. 341 |
Succinylation of Proteins | p. 343 |
Pyridylethylation of Cysteine Residues | p. 345 |
Side-Chain Selective Chemical Modifications of Proteins | p. 349 |
Nitration of Tyrosines | p. 353 |
Ethoxyformylation of Histidine | p. 357 |
Modification of Arginine Side Chains with p-Hydroxyphenylglyoxal | p. 359 |
Amidation of Carboxyl Groups | p. 361 |
Amidination of Lysine Side Chains | p. 363 |
Modification of Tryptophan with 2-Hydroxy-5-Nitrobenzylbromide | p. 365 |
Modification of Sulfhydryl Groups with DTNB | p. 367 |
Chemical Cleavage of Proteins at Methionyl Residues | p. 369 |
Chemical Cleavage of Proteins at Tryptophan Residues | p. 375 |
Chemical Cleavage of Proteins at Aspartyl Residues | p. 381 |
Chemical Cleavage of Proteins at Cysteinyl Residues | p. 385 |
Chemical Cleavage of Proteins at Asparaginyl-Glycyl Peptide Bonds | p. 389 |
Preparation of Peptides for Microsequencing from Proteins in Polyacrylamide Gels | p. 393 |
In Situ Chemical and Enzymatic Digestions of Proteins Immobilized on Miniature Hydrophobic Columns | p. 399 |
Enzymatic Digestion of Membrane-Bound Proteins for Peptide Mapping and Internal Sequence Analysis | p. 405 |
Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels | p. 415 |
Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins | p. 427 |
Peptide Mapping by Two-Dimensional Thin-Layer Electrophoresis - Thin-Layer Chromatography | p. 437 |
Peptide Mapping by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis | p. 447 |
Peptide Mapping by High-Performance Liquid Chromatography | p. 453 |
Production of Protein Hydrolysates Using Enzymes | p. 457 |
Amino Acid Analysis Using Precolumn Derivatization with 6-Aminoquinolyl-n-Hydroxysuccinimidyl Carbamate | p. 461 |
Amino Acid Analysis Using Precolumn Derivatization with Phenylisothiocyanate | p. 467 |
Molecular-Weight Estimation for Native Proteins Using Size-Exclusion High-Performance Liquid Chromatography | p. 473 |
Detection of Disulfide-Linked Peptides by HPLC | p. 479 |
Diagonal Electrophoresis for Detecting Disulfide Bridges | p. 481 |
Estimation of Disulfide Bonds Using Ellman's Reagent | p. 487 |
Quantitation of Cysteine Residues and Disulfide Bonds by Electrophoresis | p. 489 |
Detection of Disulfide-Linked Peptides by Mass Spectrometry | p. 495 |
Analyzing Protein Phosphorylation | p. 501 |
Identification of Proteins Modified by Protein (D-Aspartyl/L-Isoaspartyl) Carboxyl Methyltransferase | p. 507 |
Analysis of Protein Palmitoylation | p. 517 |
Removal of Pyroglutamic Acid Residues from the N-Terminus of Peptides and Proteins | p. 525 |
The Dansyl Method for Identifying N-Terminal Amino Acids | p. 529 |
The Dansyl-Edman Method for Peptide Sequencing | p. 535 |
Matrix-Assisted Laser Desorption Ionization Mass Spectrometry as a Complement to Internal Protein Sequencing | p. 541 |
A Manual C-Terminal Sequencing Procedure for Peptides: The Thiocyanate Degradation Method | p. 557 |
C-Terminal Sequence Analysis with Carboxypeptidase Y | p. 569 |
Rapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting | p. 573 |
Epitope Mapping of a Protein Using the Geysen (PEPSCAN) Procedure | p. 581 |
Epitope Mapping of Protein Antigens by Competition ELISA | p. 595 |
Identification of Glycoproteins on Nitrocellulose Membranes Using Lectin Blotting | p. 603 |
A Lectin-Binding Assay for the Rapid Characterization of the Glycosylation of Purified Glycoproteins | p. 619 |
Staining of Glycoproteins/Proteoglycans on SDS-Gels | p. 627 |
Chemical Methods of Analysis of Glycoproteins | p. 633 |
Monosaccharide Analysis by HPAEC | p. 635 |
Monosaccharide Analysis by GC | p. 639 |
Determination of Monosaccharide Linkage and Substitution Patterns by GC-MS Methylation Analysis | p. 641 |
Sialic Acid Analysis by HPAEC-PAD | p. 645 |
Chemical Release of O-Linked Oligosaccharide Chains | p. 647 |
O-Linked Oligosaccharide Profiling by HPLC | p. 649 |
O-Linked Oligosaccharide Profiling by HPAEC-PAD | p. 651 |
Released of N-Linked Oligosaccharide Chains by Hydrazinolysis | p. 653 |
Enzymatic Release of O- and N-Linked Oligosaccharide Chains | p. 657 |
N-Linked Oligosaccharide Profiling by HPLC on Porous Graphitized Carbon (PGC) | p. 659 |
N-Linked Oligosaccharide Profiling by HPAEC-PAD | p. 661 |
The Chloramine T Method for Radiolabeling Protein | p. 665 |
The Lactoperoxidase Method for Radiolabeling Protein | p. 669 |
The Bolton and Hunter Method for Radiolabeling Protein | p. 671 |
The Iodogen Method for Radiolabeling Protein | p. 673 |
Purification and Assessment of Quality of Radioiodinated Protein | p. 675 |
Conjugation of Peptides to Carrier Proteins via Glutaraldehyde | p. 679 |
Conjugation of Peptide to Carrier Proteins via m-Maleimidobenzoyl-N-Hydroxysuccinimide Ester (MBS) | p. 689 |
Conjugation of Peptides to Carrier Protein via Carbodiimide | p. 693 |
Raising of Polyclonal Antisera | p. 695 |
Elution of SDS-PAGE Separated Proteins from Immobilon Membranes for Use as Antigens | p. 699 |
Production of Highly Specific Polyclonal Antibodies Using a Combination of 2D Electrophoresis and Nitrocellulose-Bound Antigen | p. 703 |
Production and Characterization of Antibodies Against Peptides | p. 711 |
Production of Antibodies Using Proteins in Gel Bands | p. 717 |
Purification of IgG by Precipitation with Sodium Sulfate or Ammonium Sulfate | p. 721 |
Purification of IgG Using Caprylic Acid | p. 723 |
Purification of IgG Using DEAE-Sepharose Chromatography | p. 725 |
Purification of IgG Using Ion-Exchange HPLC/FPLC | p. 727 |
Purification of IgG by Precipitation with Polyethylene Glycol (PEG) | p. 731 |
Purification of IgG Using Protein A or Protein G | p. 733 |
Purification of IgG Using Gel-Filtration Chromatography | p. 735 |
Purification of IgG Using Affinity Chromatography on Antigen-Ligand Columns | p. 739 |
Purification of IgG Using Thiophilic Chromatography | p. 743 |
Analysis of IgG Fractions by Electrophoresis | p. 745 |
Ouchterlony Double Immunodiffusion | p. 749 |
Single Radial Immunodiffusion | p. 753 |
Rocket Immunoelectrophoresis | p. 757 |
Two-Dimensional Immunoelectrophoresis | p. 763 |
Immunogen Preparation and Immunization Procedures for Rats and Mice | p. 771 |
Hybridoma Production | p. 773 |
Screening Hybridoma Culture Supernatants Using Solid-Phase Radiobinding Assay | p. 777 |
Screening Hybridoma Culture Supernatants Using ELISA | p. 779 |
Growth and Purification of Murine Monoclonal Antibodies | p. 781 |
A Rapid Method for Generating Large Numbers of High-Affinity Monoclonal Antibodies from a Single Mouse | p. 783 |
Index | p. 793 |
Table of Contents provided by Blackwell. All Rights Reserved. |
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A remarkable treasury of 144 state-of-the-art and highly successful analytical techniques for studying proteins and peptides. John Walker has included many updated and improved methods from his best-selling Basic Protein and Peptide Protocols as well as adding nearly 100 new ones. Each tried-and-tested protocol contains detailed step-by-step instructions time-saving troubleshooting tips alternative procedures informative explanations and comprehensive lists of reagents and suppliers-aids not usually found in standard journal recipes. The techniques do not require sophisticated and expensive apparatus.
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