{"product_id":"the-protein-protocols-handbook-9781588298805","title":"The Protein Protocols Handbook","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eSince the publication of the bestselling second edition of John Walker’s widely acclaimed Protein Protocols Handbook, there have been continual methodological developments in the field of protein chemistry. This greatly enhanced third edition introduces 57 critically important new chapters, as well as significantly updating the previous edition's tried-and-true methods. Although the timely new chapters are spread throughout all of the book, the vital section on post-translational modifications has been expanded most to reflect the increasing importance of these modifications in the understanding of protein function. \u003c\/p\u003e \u003cp\u003eEach readily reproducible method follows the highly praised format of the Methods in Molecular Biology™ series, offering a concise summary of its basic theory, a complete materials list, a step-by-step protocol for its successful execution, and extensive notes on avoiding pitfalls, or on modifying the method to function within your own experimental circumstances. The expert authors of each chapter have demonstrated a hands-on mastery of the methods described, fine-tuned here for optimal productivity.\u003c\/p\u003e \u003cp\u003eComprehensive, cutting-edge, and highly practical, The Protein Protocols Handbook, Third Edition is today's indispensable benchtop manual and guide, not only for all those new to the protein chemistry laboratory, but also for those established workers seeking to broaden their armamentarium of techniques in the urgent search for rapid and robust results\u003c\/p\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003cstrong\u003ePart I : QUANTITATION OF PROTEINS\u003c\/strong\u003e \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e1. Protein Determination by UV Absorption \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and M.P. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e2. The Lowry Method for Protein Quantitation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. H. Waterborg \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e3 The Bicinchoninic Acid (BCA) Assay for Protein Quantitation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ.M. Walker\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e4 The Bradford Method for Protein Quantitation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eN.Kruger \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e5. Ultrafast Protein Determinations Using Microwave Enhancement \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. Akins and R. S. Tuan \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e6. The Nitric Acid Methods for Protein Estimation in Biological Samples \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS.A. Boerner, Y.K. Lee, S.H. Kaufmann and K. Bible\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e7. Quantitation of Tryptophan in Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and M.P. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e8. Kinetic Silver Staining of Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. D. Root and K. Wang \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e9. Quantitation of cellular proteins by flow cytometry \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eT. D. Friedrich , F.A. Ray, R.L. Smith and J. M. Lehman\u003c\/p\u003e \u003cp\u003e10. Quantitation of cellular proteins by laser scanning cytometry\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eT.D. Friedrich, R.L.Smith and J.M. Lehman \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cstrong\u003ePart II : ELECTROPHORESIS OF PROTEINS AND PEPTIDES AND DETECTION IN GELS\u003c\/strong\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e11 Protein Solubility in 2D Electrophoresis: Basic principles and issues \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eT.Rabilloud\u003c\/p\u003e \u003cp\u003e12 Mouse and Human Tissues Sample Preparation for 2-D Electrophoresis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC. Zabel and J. Klose\u003c\/p\u003e \u003cp\u003e13 Plant Protein sample preparation for 2DE \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Carpentier , R.Swennen and B. Panis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e14 Preparation of bacterial samples for 2-D PAGE. \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. Vandahl, G. Christiansen and S. Birkelund\u003c\/p\u003e \u003cp\u003e15 Preparation of bodily fluids for 2-D PAGE \u003c\/p\u003e \u003cp\u003eSullivan, H.Brzeski, J. Ganesalingam, and M. Mayr\u003c\/p\u003e \u003cp\u003e16 Immunoaffinity Depletion of high abundance plasma and serum proteins\u003c\/p\u003e \u003cp\u003eL.A. Echan and D. Speicher \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e17 Preparation of Yeast samples for 2D PAGE \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Norbeck\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e18 Membrane Protein Preparation Using Aqueous Polymer Two Phase Systems  \u003c\/p\u003e \u003cp\u003eJ. Schindler and H-G Nothwang\u003c\/p\u003e \u003cp\u003e19 Subcellular fractionation of small sample amounts \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eH.G Nothwang, I. Guillemin and J. Schindler\u003c\/p\u003e \u003cp\u003e20. Nondenaturing Polyacrylamide Gel Electrophoresis of Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ.M. Walker\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e21 SDS Polyacrylamide Gel Electrophoresis of Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ.M. Walker\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e22 Gradient SDS Polyacrylamide Gel Electrophoresis of Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ.M. Walker\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e23. SDS-Polyacrylamide Gel Electrophoresis of Peptides \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. C. Judd\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e24 Blue native gel electrophoresis (BN-PAGE) \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eElke A. Dian, J. Rassow and Christian Motz \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e25 Separation of proteins by gel electrophoresis in the Tris-Taurine-HCl system \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS.Luche, M. Chevallet C. Lelong and T. Rabilloud \u003c\/p\u003e \u003cp\u003e26 Cetyltrimethylammonium Bromide Discontinuous Gel Electrophoresis of Proteins: M -Based Separation of Proteins with Retained Native Activity\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR.E. Akins and R. S. Tuan \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e27 Acetic Acid-Urea Polyacrylamide Gel Electrophoresis of Basic Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. H. Waterborg\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e28 Acid-Urea-Triton Polyacrylamide Gel Electrophoresis of Histones \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. H. Waterborg \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e29 Isoelectric Focusing of Proteins in Ultra-Thin Polyacrylamide Gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. M. Walker\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e30 Serial immobilized pH gradient isoelectric focusing over pH 4-9 \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS.Poznanovic, W. Wozny, H. Zengerling, G.P. Schwall and M. A. Cahill \u003c\/p\u003e \u003cp\u003e31. Radiolabelling of Eukaryotic Cells and Subsequent Preparation for 2-D \u0026lt; \u003c\/p\u003e\u003cp\u003eN. Bizios\u003c\/p\u003e \u003cp\u003e32 Two-Dimensional PAGE Using Carrier Ampholyte pH Gradients in the First Dimension \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP.Gravel\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e33 Vertical agarose electrophoresis and electroblotting of high molecular weight proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Greaser and C.M. Warren\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e34 2D PAGE of high molecular weight proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Oh-Ishi and T.Maeda \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e35 Casting immobilised pH gradients \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE. Gianazza \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e36 Nonequilibrium pH Gel Electrophoresis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Carroll \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e37 Microchip capillary electrophoresis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB.A. Fogarty, N.A.Lacher and S.M. Lunte\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e38 Protein Separations in Microfluidic Chips \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Chow and B.Fathollahi \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e39 Difference gel electrophoresis (DIGE) \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. Friedman and K.S. Lilley \u003c\/p\u003e \u003cp\u003e40 Comparing 2-D Electrophoresis Gels Across Internet Databases \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP. Lemkin, G.C.Thornwall, and J.A. Evans \u003c\/p\u003e \u003cp\u003e41 Quantification of Radiolabeled Proteins in Polyacrylamide Gels 25.4.07 \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eW.R. Springer \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e42 Differential ProteoTope radioactive quantification of protein abundance ratios\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eW.Wozny, G.P.Schwall, C.S. Sastri, S.Poznanovic, W. Stegmann, Hunzinger, K. Groebe and M.A. Cahill\u003c\/p\u003e \u003col\u003e\u003cli\u003e\u003col\u003e\u003cli\u003e\n\u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e43 Quantitation of Proteins on Polyacrylamide Gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e\n\u003c\/li\u003e\u003c\/ol\u003e\u003c\/li\u003e\u003c\/ol\u003e \u003cp\u003eJ. Smith\u003c\/p\u003e \u003col\u003e\u003cli\u003e\u003col\u003e\u003cli\u003e\n\u003cp\u003e44 Using SDS-PAGE and scanning laser densitometry to measure proteins\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eAaron P. Miles and A. Saul \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e45 Rapid and Sensitive Staining of Unfixed Proteins in Polyacrylamide Gels with Nile Red \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ-R. Daban, S. B.A. Bermudez amd F.J. Alba \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e46 Zinc reverse staining technique \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC. Fernandez-Patron \u003c\/p\u003e \u003cp\u003e47 Protein Staining with Calconcarboxylic Acid in Polyacrylamide Gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eWei-Tao Cong, Sun-Young Hwang, Li-Tai Jin and Jung-Kap Choi\u003c\/p\u003e \u003cp\u003e48 Detection of Proteins in Polyacrylamide Gels by Silver Staining \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. J. Dunn \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e49 Background-free Protein Detection on Polyacrylamide Gels and on Electroblots Using Transition Metal Chelate Stains \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eW.F. Patton\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e50 Detection of Proteins in Polyacrylamide Gels by Fluorescent Staining \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. J. Dunn\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e51 Detection of Glycoproteins in Gels and Blots \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eNicolle Packer, Malcolm S Ball, Peter L Devine, and Wayne F Patton\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e52 Staining of Glycoproteins\/Proteoglycans on SDS-Gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eH.J. Møller and J.H. Poulsen \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e53. Detection of Proteins and Sialoglycoproteins in Polyacrylamide Gels Using Eosin X stain \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eF. Lin \u0026amp; G. Wise\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e54 Pro-Q Diamond phosphoprotein staining \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG.K. Agrawal and J.J. Thelen\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e55. Electroelution of Proteins from Polyacrylamide Gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP. Jenö and Martin Horst\u003c\/p\u003e \u003cp\u003e56 Autoradiography and Fluorography of Acrylamide Gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Circolo and S. Gulati\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e57 Proteolytic Activity Detection by Two-Dimensional Zymography \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ.Wilkesman \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cstrong\u003ePart III : BLOTTING AND DETECTION METHODS\u003c\/strong\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e58. Protein Blotting by Electroblotting \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R.Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e59. Protein Blotting by the Semi-dry Method \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP. Gravel \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e60. Protein Blotting by the Capillary Method \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ.M. Walker\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e61. Western Blotting of basic proteins electrophoretically resolved on acid-urea-Triton-polyacrylamide gels \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG.P. Delcuve and J. R. Davie\u003c\/p\u003e \u003cp\u003e62 Immunoblotting of 2-DE Separated Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e\n\u003c\/li\u003e\u003c\/ol\u003e\u003c\/li\u003e\u003c\/ol\u003e \u003cp\u003eMagi and L Bianchi \u003c\/p\u003e \u003col\u003e\u003cli\u003e\u003col\u003e\u003cli\u003e\u003cp\u003e\u003c\/p\u003e\u003c\/li\u003e\u003c\/ol\u003e\u003c\/li\u003e\u003c\/ol\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e63 High efficiency blotting of high-molecular weight proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Greaser and D.R. Swartz\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e64. Alkaline Phosphatase Labeling of IgG Antibody \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG. B.Wisdom \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e65. b-Galactosidase Labeling of IgG Antibody \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG. B. Wisdom \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e66. Horseradish Peroxidase Labeling of IgG Antibody \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG. B. Wisdom \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e67. Digoxigenin (DIG) Labelling of IgG Antibody \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG. B. Wisdom \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e68. Conjugation of fluorochromes to antibodies \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS-Y. Mao \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e69. Coupling of Antibodies with Biotin \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR.P. Haugland and Wendy W. You\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e70. Preparation of Avidin Conjugates \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR.P. Haugland and M.K. Bhalgat \u003c\/p\u003e \u003cp\u003e71. MDPF Staining of Proteins on Western Blots \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eF. Alba and J.R. Daban \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e72. Copper Iodided Staining of Proteins and its silver enhancement \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. D. Root and K. Wang\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e73. Detection of Proteins on Blots using Direct Blue 71 \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eWei-Tao Cong, Sun-Young Hwang, Li-Tai Jin and Jung-Kap Choi\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e74 Detection of proteins on Western blots using colorimetric and radiometric vusialization of Secondary Ligands \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eN. J. Kruger \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e75. Identification of Glycoproteins on Nitrocellulose Membranes Using Lectin Blotting\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP. Gravel \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e76. A Sensitive Method to Quantitatively Detect Total Protein on Membranes after Electrophoretic Transfer Using Avidin- or Streptavidin-Biotin \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eW.J. LaRochelle \u003c\/p\u003e \u003cp\u003e77. Detection and Quantification of Proteins on Immunoblots using Enhanced Chemiluminescence \u003c\/p\u003e \u003cp\u003eJ. Young \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e78 Reutilization of Western Blots After Chemiluminescent Detection or Autoradiography \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Kaufmann \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e79 The use of quantum dot luminescent probes for Western blot analysis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Makrides, C. Gasbarro and J.M.Bello \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e80 The use of infrared fluorescent dyes in quantitative immunoblotting \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC-H Yang, C. Kasbek, and H. A. Fisk \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e81 The use of infrared fluorescent dyes in immunofluorescence microscopy \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC. Kasbek, C-H Yang and H. A. Fisk \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cstrong\u003ePart IV : CHEMICAL MODIFICATION OF PROTEINS AND PEPTIDE \u003c\/strong\u003e\u003c\/p\u003e \u003cp\u003e\u003cstrong\u003ePRODUCTION, PURIFICATION AND CHARACTERISATION\u003c\/strong\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e82 Carboxymethylation of Cysteine Using Iodoacetamide\/Iodoacetic Acid \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and Michele Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e83 Performic Acid Oxidation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and Michele Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e84 Succinylation of Protein \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and Michele Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e85 Pyridylethylation of Cysteine Residues \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Ward\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e86. Side-Chain Selective Chemical Modifications of Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e87 Nitration of Tyrosines \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e88 Ethoxyformylation of Histidine \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e89 Modification of Arginine Side Chains with p-Hydroxyphenylglyoxal \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e90 Amidination of Carboxyl Groups  \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e91 Amidination of Lysine Side Chains \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD.S. Tawfik\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e92 Modification of tryptophan with 2-Hydroxy-5-Nitrogenzylbromide \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e93. Modification of Sulhydryl Groups with DTNB \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. S. Tawfik \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e94 Chemical Cleavage of Proteins at Methionyl-X Peptide Bonds \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB.J. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e95 Chemical Cleavage of Proteins at Tryptophanyl-X Peptide Bonds \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. J. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e96 Chemical Cleavage of Proteins at Aspartyl-X Peptide Bonds \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. J.Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e97 Chemical Cleavage of Proteins at Cysteinyl-X Peptide Bonds \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. J. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e98 Chemical Cleavage of Proteins at Asparaginyl-Glycyl Peptide Bonds \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB.J. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e99 Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels \u003c\/p\u003e \u003cp\u003eK.L. Stone, E.E.Gulcicek and K.R. Williams\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e100 On-PVDF protein digestions for N-terminal sequencing and peptide mass fingerprinting \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eVictoria Pham, William Henzel \u0026amp; Jennie R Lill\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e101 Enzymatic Digestion of Proteins on PVDF membranes \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Fernandez and S. Mische\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e102 Reverse Phase HPLC Separation of Enzymatic Digests of Proteins \u003c\/p\u003e \u003cp\u003eK.L. Stone and K.R. Williams\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e103 Peptide Mapping by Two-Dimensional Thin-Layer Electrophoresis-Thin-Layer Chromatography \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. C. Judd\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e104 Peptide Mapping by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. C. Judd\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e105 Peptide Mapping by High-Performance Liquid Chromatography \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP. Højrup \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e106 Production of Protein Hydrolysates Using Enzymes \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. M. Walker and P. J. Sweeney\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e107 Amino Acid Analysis by Precolumn Derivatization with 1- Fluoro-2,4-Dinitrophenyl-5-L-Alanine Amide (Marfey’s Reagent) \u003c\/p\u003e \u003cp\u003eS. Kochhar and P. Christen \u003c\/p\u003e \u003cp\u003e108 Amino acid analysis in protein hydrolysates using anion exchange chromatography and IPAD detection \u003c\/p\u003e \u003cp\u003eP. Jandik, Jun Cheng and N. Avdalovic \u003c\/p\u003e \u003cp\u003e109 Validation of amino acid analysis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Reason\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e110 Molecular Weight Estimation for Native Proteins Using High-Performance Size Exclusion Chromatography \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG. B. Irvine \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e111 Detection of Disulfide-Linked Peptides by HPLC \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and M. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e112 Detection of Disulfide-Linked Peptides by Mass Spectrometry \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA.Aitken and M. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e113 Diagonal Electrophoresis for Detecting Disulfide Bridges \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and M. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e114. Estimation of Disulfide Bonds Using Ellman’s Reagent \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and M. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e115 Quantitation of Cysteine Residues and Disulfide Bonds by Electrophoresis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Aitken and M. Learmonth\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e116 N-Terminal sequencing of the N-terminally Modified Proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. Kamp and Hisashi Hirano \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e117 De-blocking of Proteins containing N-Terminal Pyroglutamic Acidc\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Mozdzanowski \u003c\/p\u003e \u003cp\u003e118 Detection and characterization of protein mutations by mass spectrometry\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eY. Wada\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e119 Peptide Sequencing by Nanoelectrospray Tandem Mass Spectrometry\u003c\/p\u003e \u003cp\u003eO. Nørregaard Jensen and M. Wilm\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e120 Protein identification by Peptide mass fingerprinting using MALDI-TOFF Mass spectrometry\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Webster and D. Oxley \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e121 Protein ladder sequencing \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eRong Wang and Brian T. Chait\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e122. Sequence Analysis with WinGene\/WinPep\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eL. Hennig \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e123 HPLC and MS of integral membrane proteins\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Whitelegge \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e124 Enrichment of Serum Peptides and Analysis by MALDI-TOF Mass Spectrometry  \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eH.W. Ressom, R.S.Varghese and R. Goldman\u003c\/p\u003e \u003cp\u003e125 Computational Methods for the Analysis of MALDI-TOF Spectra to Discover Peptide Serum Biomarkers \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eY. An, H.W. Ressom and R. Goldman \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003cstrong\u003ePart V : POST-TRANSLATIONAL MODIFICATIONS\u003c\/strong\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e126 Simple tools for complex N-glycan analysis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA-C. Fitchette, M. Benchabane, T. Paccalet, L. Faye and V. Gomord\u003c\/p\u003e \u003cp\u003e127 A Lectin-Binding Assay for the Rapid Characterization of the Glycosylation of Purified Gycoproteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM.T. Goodarzi, A. Fotinopoulou and G. A. Turner\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e128 Chemical Methods of Analysis of Glycoproteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e129 Monosaccharide Analysis by HPAEC \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e130 Monosaccharide Analysis by GC \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e131 Determination of monosaccharide linkage and Substitution Patterns by GC.MS Methylation Analysis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e132 Sialic Acid Analysis by HPAEC-PAD \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e133 Chemical Release of O-Linked Oligosaccharide Chains \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e134 O-Linked Oligosaccharide Profiling by HPLC \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e135 O-Linked Oligosaccharide Profiling by HPAEC-PAD \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e136 Release of N-Linked Oligosaccharide Chains by Hydrazinolysis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eT.Mizuochi and E.F. Hounsell\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e137 Enzymatic Release of O- and N-Linked Oligosaccharide Chains \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e138 N-Linked Oligosaccharide Profiling by HPLC on Porous Graphitized Carbon (PGC) \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e139 N-linked Oligosaccharide Profiling by HPAEC-PAD \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE.F. Hounsell, M.J. Davies and K.D. Smith\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e140 HPAE-PAD analysis of monosaccharides released by exoglycosidase digestion \u003c\/p\u003e \u003cp\u003eWeitzhandler, M., J. Rohrer, J,R Thayer and N. Avdalovic \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e141 Microassay Analyses of Protein Glycosylation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eN.K.C. Wong, N. Kanu, N. Thandrayen, G,J.Rademaker, C.I. Baldwin, D.V. Renouf and E.F. Hounsell \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e142 Polyacrylamide gel electrophoresis of fluorophore-labeled carbohydrates from glycoproteins\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. Brandley, J. Klock and C. Starr \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e143 HPLC Analysis of fluorescently labelled glycans \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Merry and S. Astrautsova\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e144 Glycoprofiling purified glycoproteins using Surface Plasmon Resonance \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Fotinopoulou and G.A. Turner \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e145 Sequencing Heparan Sulphate Saccharides \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. E. Turnbull\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e146 Analysis of glycoprotein heterogeneity by Capillary Electrophoresis and Mass Spectrometry \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Hooker and D.C. James\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e147 Affinity chromatography of oligosaccharides and glycopeptides with immobilized lectins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eK. Yamamoto \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e148 In-Gel Enzymatic Release of N-glycans \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. Harvey\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e149 Analysis of N-Linked glycans by mass spectrometry \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD. Harvey\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e150 MS Analysis of Protein glycosylation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eN.Takemori, N. Komori and H. Matsumoto \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e151 Mapping protein N-glycosylation by COFRADIC \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. Ghesquiere, J. Vandekerckhove, and K. Gevaert \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e152 Mass spectrometric analysis of O-linked glycans released directly from Glycoproteins in gels using ß-elimination \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA.M. Taylor and J. Thomas-Oates \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e153 Glycopeptide analysis using LC\/MS and LC\/MS\u003csup\u003en\u003c\/sup\u003e \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS.Itoh, D. Takakura, N. Kawasaki and T. Yamaguchi \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e154 Identification of Vitamin K-Dependent Proteins Using a Gla-specific Monoclonal Antibody \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eK. Hansson \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e155 The identification of protein S-Nitrocysteine \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eT.M Greco, S.L.Stamer, D.C. Liebler and H. Ischiropoulos \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e156 Detection of nitrotyrosine-containing proteins \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eXianquan Zhan and D. Desiderio \u003c\/p\u003e \u003cp\u003e157 Mass spectrometric determination of protein Ubiquitination \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC. E. Parker, M.R.E. Warren, V. Mocanu, S.F. Greer and C.H. Borchers\u003c\/p\u003e \u003cp\u003e158 Detection of Sumoylated Proteins\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eOk-Kyong Park-Sarge and K. Sarge \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e159 Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Dubrovska \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e160 Analyzing Protein Phosphorylation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJ. Colyer\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e161 Mass spectrometric analysis of protein phosphorylation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Gander, A. Cremonesi, J. Chicher, S. Moes and P. Jenö \u003c\/p\u003e \u003cp\u003e162 Protein microarrays for phosphorylation studies\u003csup\u003e \u003c\/sup\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eB. Kersten and T. Feilner \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e163. Two Dimensional Phosphopeptide Mapping \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eH. Nagahara, R.R. Latek, S.A. Ezhevsky and S.F. Dowdy \u003c\/p\u003e \u003cp\u003e164 Identification of Proteins Modified by Protein (D-Aspartyl\/L-Isoaspartyl) Carboxyl Methyltransferase \u003c\/p\u003e \u003cp\u003eD. Weber and P.N. McFadden\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e165 Analysis of Tyrosine-o- sulfation \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eJens R. Bundgaard, J.W. Sen, A.H. Johnsen and J.F. Rehfeld \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e166 Analysis of Protein Palmitoylation by metabolic radiolabeling methods \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eK.H. Pedone, L.S. Bernstein, Maurine E. Linder and J.R. Hepler\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e167 Incorporation of radiolabeled prenyl alcohols and their analogs into mammalian cell proteins: a useful tool for studying protein prenylation\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Corsini, C.C. Farnsworth, P. McGeady, M.H. Gelb and J.A. Glomset\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e168 Labelling and analysis of isoprenylated proteins in cells \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eD.A. Andres, D.C. Crick, H.P.Spielmann and C. J. Waechter\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cstrong\u003ePart VII : ANTIBODY TECHNIQUES\u003c\/strong\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e169 Antibody Production \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. Burns\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e170 Production of Antibodies Using Proteins in Gel Bands \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS.A. Amero, T.C. James and S.C.R. Elgin\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e171 Raising Highly Specific Polyclonal Antibodies Using Biocompatible Support \u003c\/p\u003e \u003cp\u003eBound Antigens \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Diano and A. Le Bivic\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e172 Production of antisera using peptide conjugates \u003c\/p\u003e \u003cp\u003eT. E. Adrian\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e173 Small-molecule protein conjugation procedures \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Thompson \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e174 The Chloramine T Method for Radiolabeling Protein \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG.S. Bailey\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e175 The Lactoperoxidase Method for Radiolabeling Protein \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG.S. Bailey\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e176 The Bolton and Hunter Method for Radiolabeling Protein \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG.S. Bailey\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e177 Preparation of \u003csup\u003e125\u003c\/sup\u003eI-labelled peptides and proteins with high specific activity \u003c\/p\u003e \u003cp\u003eusing iodogen \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Conlon \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e178 Purification and Assessment of Quality of Radioiodinated Protein \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG.S. Bailey\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e179 Purification of IgG by Precipitation with Sodium Sulfate or Ammoniun Sulfate\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e180 Purification of IgG Using Caprylic Acid \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e181 Purification of IgG Using DEAE-Sepharose Chromatography \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e182 Purification of IgG Using Ion-Exchange HPLC \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e183 Purification of IgG by Precipitation with Polyethylene Glycol (PEG)  \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e184 Purification of IgG Using Protein A or Protein G \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e185 Purification of IgG Using Size Exclusion High Performance Liquid \u003c\/p\u003e \u003cp\u003eChromatography (SE-HPLC) \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC. Dolman and R. Thorpe \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e186 Purification of IgG Using Affinity Chromatography on Antigen-Ligand \u003c\/p\u003e \u003cp\u003eColumns \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e187 Purification of IgG Using Thiophilic Chromatography\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e188 Analysis of IgG Fractions by Electrophoresis \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e189 Purification of Immunoglobulin Y (IgY) from Chicken Eggs \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC.R. Bird and R. Thorpe \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e190 Affinity Purification of Immunoglobulins Using PAM (Protein A Mimetic)\u003c\/p\u003e \u003cp\u003eG. Fassina G. Palombo, A. Verdoliva and M. Ruvo\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e191 Detection of Serological Cross Reactions by Western Cross Blotting \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eP. Hemmerl, A. Hartl, J. Freund and J.Thalhamer \u003c\/p\u003e \u003cp\u003e192 Enzymatic Digestion of Monoclonal Antibodies \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Andrew\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e193 How to Make Bispecific Antibodies \u003c\/p\u003e \u003cp\u003eR. French\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e194 Antigen Measurements Using ELISA \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eW. Jordan\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e195 Enhanced chemiluminescence immunoassay \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. Stott\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e196 Immunoprecipitation and Blotting \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eS. Thompson \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e197 Determination of Epitope by Mass Spectrometry \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eC.Hager-Braun and K. B. Tomer \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e198 Immunogen Preparation and Immunization Procedures for Rats and Mice \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e199 Making Hybridomas \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eR. Burns\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e200 Growing hybridomas \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eG. Entrican, C. Jepson and D. Deane\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e201 Mouse Hybridomas as an Entryway to Monoclonal Antibody Design \u003c\/p\u003e \u003cp\u003eand Production \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE. Mechetner\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e202 Pitfalls \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eE. Mechetner\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e203 Recombinant antibody expression and purification \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\u003cp\u003eA. Knappik and R. Brundiers\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e204 Screening Hybridoma Culture Supernatants Using Solid-Phase Radiobinding \u003c\/p\u003e \u003cp\u003eAssay \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e205 Screening Hybridoma Culture Supernatants Using ELISA \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e206 Growth and Purification of Murine Monoclonal Antibodies \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eM. Page and R. Thorpe\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e207 Affinity purification techniques for monoclonal antibodies \u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eA. Schwarz\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e208 A rapid method for generating large numbers of high-affinity monoclonal antibodies from a single mouse\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003eN.T. Man and G.E. Morris \u003c\/p\u003e","brand":"Humana Press Inc.","offers":[{"title":"Default Title","offer_id":51041529594199,"sku":"9781588298805","price":224.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781588298805.jpg?v=1750950652","url":"https:\/\/bookcurl.com\/products\/the-protein-protocols-handbook-9781588298805","provider":"Book Curl","version":"1.0","type":"link"}