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Antigen Antibody Interactions

  • Book
  • © 1976

Overview

Authors:
  1. Charles DeLisi

    1. Department of Health, Education and Welfare Public Health Service, National Institutes of Health, Bethesda, USA

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Part of the book series: Lecture Notes in Biomathematics (LNBM, volume 8)

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Table of contents (8 chapters)

  1. Front Matter

    Pages I-IV
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  2. Introduction

    • Charles DeLisi
    Pages 1-8

  3. Hinge and Valence Effects on Antibody Binding Properties

    • Charles DeLisi
    Pages 9-32

  4. Combining Site Heterogeneity. The Free Energy Distribution Function

    • Charles DeLisi
    Pages 33-46

  5. Combining Site Heterogeneity. Immunodiffusion

    • Charles DeLisi
    Pages 47-61

  6. The Theory of Plaque Growth Kinetics for a Lymphocyte Source

    • Charles DeLisi
    Pages 62-82

  7. Plaque Inhibition: Growth Kinetics in the Presence of Competitive Interactions

    • Charles DeLisi
    Pages 83-102

  8. Applications of Plaque Growth Theory and Immunological Implications

    • Charles DeLisi
    Pages 103-112

  9. Dynamical Phenomena on Lymphocyte Membranes

    • Charles DeLisi
    Pages 113-137

  10. Back Matter

    Pages 138-144
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Keywords

About this book

1. 1 Organization of the Immune System One of the most important survival mechanisms of vertebrates is their ability to recognize and respond to the onslaught of pathogenic microbes to which they are conti- ously exposed. The collection of host cells and molecules involved in this recognitionยญ 12 response function constitutes its immune system. In man, it comprises about 10 cells 20 (lymphocytes) and 10 molecules (immunoglobulins). Its ontogenic development is c- strained by the requirement that it be capable of responding to an almost limitless variety of molecular configurations on foreign substances, while simultaneously remaining inert to those on self components. It has thus evolved to discriminate, with exquisite precision, between molecular patterns. The foreign substances which induce a response, called antigens, are typically large molecules such as proteins and polysaccharides. The portions of these with which immunoglobulins interact are called epitopes or determinants. A typical protein epitope may consist of a configuration formed by the spatial arrangements of four or five amino acids and have an average linear dimension of about 20 A.

Authors and Affiliations

  • Department of Health, Education and Welfare Public Health Service, National Institutes of Health, Bethesda, USA

    Charles DeLisi

Bibliographic Information

  • Book Title: Antigen Antibody Interactions

  • Authors: Charles DeLisi

  • Series Title: Lecture Notes in Biomathematics

  • DOI: https://doi.org/10.1007/978-3-642-93044-7

  • Publisher: Springer Berlin, Heidelberg

  • eBook Packages: Springer Book Archive

  • Copyright Information: Springer-Verlag Berlin ยท Heidelberg 1976

  • Softcover ISBN: 978-3-540-07697-1Published: 01 June 1976

  • eBook ISBN: 978-3-642-93044-7Published: 13 March 2013

  • Series ISSN: 0341-633X

  • Series E-ISSN: 2196-9981

  • Edition Number: 1

  • Number of Pages: IV, 142

  • Topics: Mathematics, general

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