M. Zouhair Atassi
Springer US
1977e druk, 2011
9781461341925
Immunochemistry of Proteins
Volume 1
Specificaties
Paperback, 486 blz.
|
Engels
Springer US |
1977e druk, 2011
ISBN13: 9781461341925
Rubricering
Levertijd ongeveer 8 werkdagen
Samenvatting
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 Land steiner 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 is 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 1960s to enable the successful 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 of the immunochemistry of homo- or mixed amino acid polymers in the hope that the information derived from these systems might prove useful in the understanding of the immunochemistry of proteins.
Specificaties
ISBN13:9781461341925
Taal:Engels
Bindwijze:paperback
Aantal pagina's:486
Uitgever:Springer US
Druk:1977
Inhoudsopgave
1 Chemical Modification and Cleavage of Proteins and Chemical Strategy in Immunochemical Studies of Proteins M. Z. Atass.- I. Introduction.- A: Chemical Modification Reactions.- II. Usefulness and Limitations.- III. Choice of Reaction and Evaluation of Results.- IV. Modification Reactions of Various Side Chains.- A. Reactions for Amino Groups.- B. Reactions for Aliphatic Hydroxyls.- C. Reactions for Arginine.- D. Reactions for Carboxyl Groups.- E. Reactions for Histidine.- F. Reactions for Methionine.- G. Reactions for Sulfhydryl (Thiol) Groups.- H. Reactions for Disulfide Bonds.- I. Reactions for Tryptophan.- J. Reactions for Tyrosine.- K. Cross-Linking Reagents.- L. Affinity-Labeling (Active-Site-Directed) Reagents.- B: Chemical Cleavage Reactions.- V. Usefulness, Limitations, and Evaluation of the Results.- VI. Choice of Reaction.- VII. Cleavage Reactions.- A. N-Terminal Removal.- B. Cleavage at Carboxyl and Carboxamide Groups.- C. Cleavage at Cysteine Peptide Bonds.- D. Cleavage at Cystine Peptide Bonds.- E. Cleavage at Histidine Peptide Bonds.- F. Cleavage at Aliphatic Hydroxy 1 Groups.- G. Cleavage of Methionine Peptide Bonds.- H. Cleavage of Proline Peptide Bonds.- I. Cleavage of Tryptophan Peptide Bonds.- J. Cleavage at Tyrosine Peptide Bonds.- K. Miscellaneous Addition and Cleavage Reactions.- L. Modified Enzymatic Cleavage.- VII. References.- 2 Influence of Conformation on Immunochemical Properties of Proteins.- I. Introduction.- II. Factors Responsible for Protein Folding.- A. Factors Intrinsic to the Protein Molecule.- B. Dependence of Protein Conformation on Environment.- III. Dependence of Conformation on the Whole Amino Acid Sequence: Conformation of Unique Protein Fragments.- IV. Use of Immunochemical Methods as a Conformational Probe.- A. Influence of Evolutionary Amino Acid Replacements on Conformation.- B. Conformational Equilibrium in Protein Fragments.- V. Influence of Conformational Changes on Immunochemical Behavior.- A. Conformational Changes Induced by Modification of Nonimmunogenic Prosthetic Groups.- B. Conformational Changes Induced by Controlled Modification of Amino Acid Residues.- VI. Conclusion.- VII. References.- 3 Investigation of Immunochemical Reactions by Fluorescence Polarization.- I. Introduction.- II. Symbols.- III. Equations Relating Fluorescence Polarization and Intensity to Concentration.- IV. Equilibrium Equations.- A. Classical Mass Law, Uniformly Binding Sites, No Site-Site Interactions.- B. Nonuniformly Binding Sites Characterized by a Sips Distribution of Binding Affinities.- V. Kinetic Equations.- A. Reaction Order.- B. Evaluation of Rate Constants.- C. Dissociation of Complexes.- VI. Relaxation Methods.- VII. Results Obtained on Immunochemical Reactions by Means of Fluorescence Polarization and Intensity Measurements.- A. Determination of Binding Affinities and Site Concentration from Equilibrium Titrations.- B. Immunoassay.- C. Determination of Reaction Order.- D. Determination of the Forward- and Back-Reaction Rate Constants.- E. Activation Parameters.- VIII. What Has Been Learned from Fluorescence Polarization Measurements on Antigen-Antibody and Hapten-Antibody Reactions?.- A. Antibody Binding Affinity and Specificity.- B. Antibody “Maturation” during the Immune Response....- C. Effects of Fluorescent Labeling upon Immunochemical Reactivity.- D. Why Does Antifluorescein Quench the Fluorescence of Fluorescein?.- E. The Mechanism of Antigen-Antibody and Hapten- Antibody Reactions.- F. Specific Ionic Effects on Reaction Rates and Activation Parameters.- G. Manipulation of the Binding Affinity of Antibody by Changing Either the Forward- or Backward-Rate Constants of the Binding Reaction.- IX. References.- 4 In Vitro Immune Responses of Lymphoid Cell Populations to Proteins and Peptides.- I. Introduction.- A. Scope.- B. Historical.- II. In Vitro Consequences of the Reaction of Proteins or Peptides with Lymphoid Cell Populations.- A. Cellular Events, Requirements, and Kinetics of Responses to Proteins.- B. In Vitro Immunological Responses to Peptides.- C. Roles of Persisting Immunogen and Accessory and Thymus-Derived Cells in the Maintenance of the Antibody Response.- D. Regulation of the Antibody Response.- III. Induction and Regulation of in Vitro Immune Responses by Soluble Factors.- A. Production of Soluble Factors from T Cells.- B. Soluble Factors with Helper and/or Regulatory Activity Generated by or Prepared from T Lymphocytes.- IV. Discussion.- A. Antigen-Binding Receptors on Lymphocytes.- B. Cellular and Molecular Aspects of Induction.- C. Maintenance of the Antibody Response.- D. Nonspecific Induction and Regulation of the Antibody Response.- E. Future Outlook.- V. References.- 5 Immunochemistry of Encephalitogenic Protein.- I. Introduction.- A. Characteristics of Experimental Allergic Encephalomyelitis.- B. The Autoimmune Component(s).- II. Nature and Properties of Encephalitogenic Protein.- A. Localization and Biochemical Characteristics.- B. General Immunological Aspects.- III. Antigenic Determinants with Disease-Inducing Properties.- A. The Tryptophan-Containing Region.- B. Region 46–91.- C. The N-Terminal Region.- D. The C-Terminal Region.- IV. Antigenic Determinants Connected with Protection against Disease.- V. Antigenic Determinants Connected with Cell-Mediated Immunity.- A. Delayed-Type Hypersensitivity in Vivo.- B. Tests in Vitro.- VI. Antigenic Determinants for the Humoral Immune Response...- VII. Concluding Remarks.- VIII. References.- 6 Immunochemistry of Collagen.- I. Chemical and Structural Considerations of Collagen.- II. Immunochemistry of Collagen.- A. Rat Collagen.- B. Calf Collagen.- C. Human Collagen.- D. Guinea Pig Skin Collagen.- E. Fish Collagen.- F. Invertebrate Collagens.- G. Collagens of Types II, III, and IV.- H. Modified Collagens and Collagenlike Synthetic Peptides….- I. General Considerations.- III. Cell-Mediated Immunity to Collagen.- IV. Genetic Control of the Immune Response to Collagen.- V. Antibodies to Procollagen.- VI. Applications of Collagen Immunochemistry to Medical Research.- VII. References.- 7 Histocompatibility Antigens.- I. The HL-A System of Man.- II. Alloantigens of the Mouse.- A. H-2 Complex of the Mouse.- B. Other Antigen-Determining Loci of the Mouse H-.- Complex.- C. Ia Antigens and Ir Genes.- III. Purification Methods for H-2 and HL-A Alloantigens.- A. Cell Disruption.- B. Papain Solubilization.- C. Lectin Affinity Column.- D. Detergent Solubilization.- E. Solubilization by Sonication.- F. 3 M KC1 Extraction.- G. Molecular Sizes Encountered in Isolation.- IV. Chemical Nature of H-2 and HL-A Antigens.- A. Protein Nature.- B. Carbohydrate Content.- C. ?2-Microglobulin.- V. Conclusion.- VI. References.- Author Index.