Immunochemistry of Proteins: Volume 2

ISBN-13: 9781461341956 / Angielski / Miękka / 2011 / 438 str.

M. Atassi

Opis

The structural features responsible for the immunogenicity of certain parts of native protein molecules have been of interest to immunochemists and protein chemists for over three decades. Following the early work of Landsteiner in 1942, which showed that peptide fragments from silk fibroin exhibited an inhibitory activity toward the reaction of the protein with its antibodies, fragments from many other protein systems have been isolated and studied. However, no concerted effort was (or could be) devoted to the elucidation of the complete antigenic structure of a protein. In order for these endeavors to be successful and meaningful, knowledge of both the amino acid sequence and the detailed three-dimensional structure of the protein are necessary. Such information was not available for a protein until early in the 1960s. This and the fact that protein chemistry was not in fact sufficiently developed early in the 1 960s to enable the success- ful completion of the entire antigenic structure of a protein were major contributing factors for the slow progress in this field. Determination of the antigenic structures of proteins, therefore, posed a chemical challenge of enormous proportions. For these reasons, many investigators diverted their attention to study the immunochemistry of homo- or mixed amino acid polymers in the hope that the information derived from these systems may prove useful in the understanding of the immunochemistry of proteins. A great many data on these systems were accumulated that have proved valuable in gaining some information on the immune mechanism.

Spis treści

1 Affinity Chromatography in Immunology.- I. Introduction.- II. Selection of Matrix.- III. Chemistry of Immobilization.- A. General.- B. Cyanogen Bromide Method for Activating Agarose..- C. Introduction of Various Functional Groups.- D. Stable Activated Agarose Derivatives.- E. Stability of Immobilized Ligands—The Problem of Leakage.- F. Solutions to the Leakage Problem.- G. The Concept of Multipoint Attachment of Ligand..- H. Methods Alternative to Cyanogen Bromide.- IV. Elution Techniques.- A. General Considerations.- B. Hydrophobic Binding.- C. Denaturing and Chaotropic Agents.- D. Other Eluting Agents.- E. Miscellaneous Methods.- V. Purification of Antigens.- A. General Considerations.- B. Isolation of Affinity-Labeled Peptides.- C. Isolation of Lipoprotein Subpopulations.- D. Clostridium pertringens Enterotoxin.- E. Human Chorionic Somato-Mammotropin.- F. Luteinizing Hormone.- G. Glucagonlike Immunoreactivity.- H. Isoprothrombin and Prothrombin.- I. Complement Components.- J. Transamidase.- K. Viruses.- VI. Purification of Antibodies.- A. Mono- and Oligosaccharides.- B. Ganglioside Adsorbents.- C. Plant Lectins.- D. Insulin.- E. Polypeptide Chains of a Protein.- F. Hemoglobins.- G. Angiotensin II.- H. Polyamino Acids.- I. Viral Antibodies.- VII. Separation of Cell Populations.- VIII. Reversed Affinity Chromatography.- IX. Miscellaneous Applications.- A. Immobilized Lectins as Immunoadsorbents.- B. Miscellaneous Examples.- X. References.- 2 The Effect of Antigen Structure on Preferential Humoral or Cellular Immunogenicity.- I. Introduction.- II. Antigenic Specificity.- III. Immune Induction.- IV. The Effect of Determinant Valency.- V. References.- 3 The Complete Antigenic Structure of Myoglobin: Approaches and Conclusions for Antigenic Structures of Proteins.- I. Introduction.- II. Strategy of Approach.- A. Effect of Conformational Changes on the Immunochemical Behavior.- B. Immunochemistry of Specific Chemical Derivatives.- C. Immunochemistry of Overlapping Peptides.- D. Specifically Modified Derivatives of Immunochemically Reactive Peptides.- E. Accurate Delineation of Reactive Regions by Immunochemical Studies of Synthetic Peptides.- III. Accurate Assignment of the Reactive Regions.- A. Delineation of the Reactive Region in Sequence 1–55.- B. The Reactive Region in Sequence 54–87.- C. The Reactive Region in Sequence 83–103.- D. The Reactive Region in Sequence 104–120.- E. The Reactive Region in Sequence 120–153.- IV. Contribution of the Reactive Regions to the Total Immune Reaction of Myoglobin and Immunochemical Independence of the Regions.- A. Do the Five Reactive Regions Account for the Entire Reaction of Myoglobin?.- B. Immunochemical Independence of the Regions.- V. In Vitro Studies with the Synthetic Regions.- VI. Immunochemical Relationship of Myoglobins and Nature of Immunochemical Cross-Reactions of Proteins.- A. Cross-Reactions of Some Mammalian Myoglobins and Influence of Conformation on the Immunochemistry.- B. Cross-Reaction between Sperm Whale and Finback Whale Myoglobins.- VII. Conclusions.- A. Special Features of the Antigenic Structure of Mb.- B. Conclusions Relating to Antigenic Structures of Proteins.- C. Closing Remarks.- VIII. References.- 4 The Antigenic Structure of Hen Egg-White Lysozyme: A Model for Disulfide-Containing Proteins.- I. Introduction.- II. Immunochemistry and Conformation of Lysozyme Derivatives with Broken Disulfide Bonds.- A. Accessibility of the Disulfide Bonds and Their Re-formation.- B. Effect of Disulfide Bond Cleavage on the Immunochemistry.- III. Immunochemistry and Conformation of Specific Chemical Derivatives of Lysozyme.- A. Tyrosine Derivatives.- B. Tryptophan Derivatives.- C. Arginine Derivatives.- D. Methionine Derivatives.- E. Carboxyl Group Derivatives.- F. Amino Group Derivatives.- G. Other Lysozyme Derivatives.- IV. Immunochemistry of Peptide Fragments.- A. Peptides Obtained by Peptic and Other Cleavage Procedures.- B. A Novel Cleavage Approach That Yielded Fragments Accounting for the Full Antigenic Reactivity.- V. Specific Chemical Derivatives of Immunochemically Reactive Reactive Peptides.- A. Derivatives of the Two-Disulfide Peptide.- VI. Peptide Synthesis for Final Delineation of Antigenic Sites..- VII. Accurate Assignment of the Antigenic Sites.- A. The Reactive Site around the Disulfide 6–127 (Site 1).- B. The Reactive Site around the Disulfides 64–80 and 76–94 (Site 2).- C. The Reactive Site around the Disulfide 30–115 (Site 3).- D. Contribution of the Three Sites to the Total Immune Reactivity of Lysozyme.- VIII. Immunochemistry of Lysozymes from Various Species and Other Closely Related Proteins.- A. Structural and Immunochemical Relationships of Lysozymes from Various Species.- B. Structural and Immunochemical Relationship of Lysozyme and ?-Lactalbumin.- IX. Conclusions.- A. Summary of the Features of the Antigenic Structure.- B. Closing Remarks.- X. References.- 5 Immunochemistry of the Tobacco Mosaic Virus Protein.- I. Introduction.- A. The Tobacco Mosaic Virus Protein — Physicochemical Characteristics.- II. The Relationship between Antigenic Structure and Binding with Antibodies.- A. Isolation and Characterization of an Antigenic Area of the Tobacco Mosaic Virus Protein.- B. The Synthesis of Antigenic Peptides.- C. Serological Specificity: Antigenic Properties of Synthetic Analogs.- III. The Relationship between Antigenic Structure and Cell-Mediated Immunity.- A. Delayed Hypersensitivity.- B. Production of Migration Inhibitory Factor.- IV. The Relationship between Structure and Immunogenicity.- A. Immunogenicity of Nonconjugated Peptides.- B. Immunogenicity of Peptide—Carrier Conjugates.- V. The Genetic Control of the Immune Responsiveness to Antigenic Areas of TMVP.- A. Differences in Antibody Specificity.- B. “Allotype Associated” Genetic Control of Immune Responsiveness to an Antigenic Peptide of TMVP.- VI. Concluding Remarks.- VII. References.- 6 Immunochemistry of Protein Mutants.- I. Introduction.- A. Effect of Sequence Changes on Conformation of Globular Proteins of a Homologous Set.- B. The Relationship between Sequence Changes and Antigenicity in Proteins.- II. Immunochemical Detection of Single Amino Acid Differences in Proteins.- A. Evaluation of Different Measurements of Antigenicity.- B. Relationship of Sequence Differences between Immunogen and Structure of Homologous Protein in Immunized Recipient.- III. Relationship of Immunogenicity to Single Amino Acid Differences in Proteins.- A. An Evaluation of How Much Sequence Dissimilarity between Immunogen and Homologous Protein in Immunized Recipient Is Associated with an Immune Response.- B. Comparison of Antigenic Specificities of Primary and Secondary Immune Responses.- IV. Isolation of Antibodies Sensitive to Single Amino Acid Differences in Protein Antigens.- A. Procedure of Isolation.- B. Structural and Functional Properties of “Site Specific” Antibodies.- V. Fractionation of an Antibody Response by Methods Other Than Immunoadsorbents Related to Single Amino Acid Differences.- A. Taking Advantage of Inequalities in the Concentrations of the Various Antibody Populations.- B. By Affinity Chromatography Columns Made with Antigenically Active Peptides.- C. By Taking Advantage of Special Specificities.- VI. Speculations on the Relationship of Protein Antigenicity and Antigen Receptors on T and B Cells.- VII. References.- 7 Evolution of the Immunogenic and Subunit Interaction Sites of Oligomeric Enzymes.- I. Introduction.- II. Theoretical Considerations on the Evolution of Enzymes.- A. Primary Events: Gene Duplication and Mutation.- B. Consequences.- III. Experimental Examples.- A. Monomeric Enzymes.- B. The Immunoglobulins and Dehydrogenases.- C. Review of Antigenicity and Subunit Interaction.- D. Retention of Immunogenic Homology.- E. Retention of Subunit Interaction Homology.- IV. Concluding Remarks and Prognosis.- V. References.- 8 The Structure and Activity of Concanavalin A.- I. Introduction and Biological Properties.- II. Carbohydrate Binding Specificity.- A. Precipitation with Polysaccharides.- B. Hapten Inhibition Studies.- C. Internal 2-O-Substituted ? -d-Mannopyranosyl Residues Also Interact with Concanavalin A.- D. A Hydrophobic Site Adjacent to the Carbohydrate-Specific Binding Site.- III. Chemical Modification Studies.- IV. Three-Dimensional Structure.- A. Subunit Composition.- B. Monomer.- C. Dimer.- D. Tetramer.- E. The Manganese and Calcium Binding Sites.- F. Apoconcanavalin A.- G. Nonpolar Binding Cavity.- H. The Carbohydrate Binding Site.- I. Comparison with Other Structures.- V. References.- Author Index.