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Showing 341-359 of 359 results
  1. Web-based Computational Tools for the Prediction and Analysis of Post-translational Modifications of Proteins

    The increase in the number of Web-based resources on post-translational modification sites (PTMSs) in proteins is accelerating. The paper presents a...
    Vladimir A. Ivanisenko, Dmitry A. Afonnikov, Nikolay A. Kolchanov in Post-translational Modifications of Proteins
    Protocol 2008
  2. Analysis of S-Acylation of Proteins

    Palmitoylation or S-acylation is the post-translational attachment of fatty acids to cysteine residues and is common among integral and peripheral...
    Michael Veit, Evgeni Ponimaskin, Michael F. G. Schmidt in Post-translational Modifications of Proteins
    Protocol 2008
  3. Separation of N-Glycans by HPLC

    Most glycoproteins carry a very heterogeneous mixture of oligosaccharides and even a single glycosylation site of a pure glycoprotein is often...
    Martin Gohlke, Véronique Blanchard in Post-translational Modifications of Proteins
    Protocol 2008
  4. Comparability and Monitoring Immunogenic N-linked Oligosaccharides from Recombinant Monoclonal Antibodies from Two Different Cell Lines using HPLC with Fluorescence Detection and Mass Spectrometry

    One of the most important structural features of recombinant monoclonal antibodies produced in mammalian cells is the N-linked oligosaccharide...
    Bruce R. Kilgore, Adam W. Lucka, ... Shirish T. Dhume in Post-translational Modifications of Proteins
    Protocol 2008
  5. Enzymatical Hydrolysis of N-Glycans from Glycoproteins and Fluorescent Labeling by 2-Aminobenzamide (2-AB)

    When performing a structural analysis of N-glycans, a number of aspects should be considered. N-Glycans may be hydrolyzed from purifi ed...
    Protocol 2008
  6. α-Amidated Peptides: Approaches for Analysis

    α-Amidation is a terminal modification in peptide biosynthesis that can itself be rate-limiting in the overall production of bioactive α-amidated...
    Gregory P. Mueller, William J. Driscoll in Post-translational Modifications of Proteins
    Protocol 2008
  7. Detection and Analysis of Protein ISGylation

    ISG15 is a ubiquitin-like modifi er that is conjugated to target proteins by a sequential reaction catalyzed by E1/E2/E3 enzymes (protein...
    Tomoharu Takeuchi, Hideyoshi Yokosawa in Post-translational Modifications of Proteins
    Protocol 2008
  8. Identification of Protein Phosphorylation Sites by Advanced LC-ESI-MS/MS Methods

    Phosphorylation, the process by which a phosphate group is attached to a pre-existing protein, is an evolutionarily and metabolically cheap way to...
    Christoph Weise, Christof Lenz in Post-translational Modifications of Proteins
    Protocol 2008
  9. Analysis of Methylation, Acetylation, and other Modifications in Bacterial Ribosomal Proteins

    A wide variety of post-translational modifications of expressed proteins are known to occur in living organisms (1). Although their presence in an...
    Randy J. Arnold, William Running, James P. Reilly in Post-translational Modifications of Proteins
    Protocol 2008
  10. Analysis of Sumoylation

    Reversible attachment of SUMO (small ubiquitin related modifi er) regulates a large number of proteins and plays an important role in processes such...
    Protocol 2008
  11. Disulfide Bond Map** by Cyanylation-induced Cleavage and Mass Spectrometry

    Oxidation of sulfhydryl groups to form a disulfi de bond is one of the most common post-translational modifi cations in proteins. Disulfi de bonds...
    Protocol 2008
  12. Characterization of Site-specific N-Glycosylation

    Even if a consensus sequence has been identified for a post- translational modification, the presence of such a sequence motif only indicates the...
    Katalin F. Medzihradszky in Post-translational Modifications of Proteins
    Protocol 2008
  13. Monitoring Glycosylation of Therapeutic Glycoproteins for Consistency by HPLC Using Highly Fluorescent Anthranilic Acid (AA) Tag

    Majority of protein drugs in development today are glycoproteins e.g. recombinant antibodies expressed in various cell lines. Oligosaccharides...
    Shirish T. Dhume, George N. Saddic, Kalyan R. Anumula in Post-translational Modifications of Proteins
    Protocol 2008
  14. Analysis of Tyrosine-O-Sulfation

    Tyrosine O-sulfation was first described about 50 years ago as a post-translational modification of fibrinogen. In the following 30 years it was...
    Jens R. Bundgaard, Jette W. Sen, ... Jens F. Rehfeld in Post-translational Modifications of Proteins
    Protocol 2008
  15. Mass Spectrometric Determination of Protein Ubiquitination

    Mass spectrometric methods of determining protein ubiquitination are described. Characteristic mass shifts and fragment ions indicating ubiquitinated...
    Carol E. Parker, Maria R. E. Warren, ... Christoph H. Borchers in Post-translational Modifications of Proteins
    Protocol 2008
  16. Mass Spectrometry and HPLC with Fluorescent Detection-Based Orthogonal Approaches to Characterize N-Linked Oligosaccharides of Recombinant Monoclonal Antibodies

    A number of HPLC and mass spectrometric techniques are used to characterize post-translational modification in recombinant monoclonal antibodies...
    Adam W. Lucka, Bruce R. Kilgore, ... Shirish T. Dhume in Post-translational Modifications of Proteins
    Protocol 2008
  17. Detection of Post-translational Modifications by Fluorescent Staining of Two-Dimensional Gels

    Post-translational modifications (PTMs) are key to the regulation of functional activities of proteins. Quantitative and qualitative information...
    Archana M. Jacob, Chris W. Turck in Post-translational Modifications of Proteins
    Protocol 2008
  18. Enzymatic Sequence Analysis of N-Glycans by Exoglycosidase Cleavage and Mass Spectrometry – detection of Lewis X Structures

    Enzymatic sequencing of oligosaccharides gives structural information on sequence of monosaccharides and type of linkage within the oligosaccharide...
    Christoph Kannicht, Detlef Grunow, Lothar Lucka in Post-translational Modifications of Proteins
    Protocol 2008
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