MICR 2420 Lecture Notes - Lecture 20: Pentamer, Immunoglobulin D, Ferris Wheel

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Antibodies- Types, Structures,
Functions.
Joan L. Slonczewski and John W. Foster
Microbiology:
An Evolving Science
FOURTH EDITION
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Antibodies
24.2 Antibody Structure, Diversity
Learning Objectives
24.2.a. Assess how the structure of an antibody relates to its function.
24.2.b. Compare and contrast the five antibody classes.
24.2.c. Distinguish among isotype, allotype, and idiotype.
24.2.d. Differentiate between the primary and secondary antibody
responses.
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Antibody Structure & Diversity,
Antibodies, also called immunoglobulins, are
members of the larger immunoglobulin superfamily
of proteins.
-Made by the body in response to an antigen,
antibodies are the keys to immunological
specificity.
Like miniature “smart bombs,” antibody
immunoglobulins individually circulate through
blood, ignoring all antigens except those for which
they were designed.
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Document Summary

Assess how the structure of an antibody relates to its function. Differentiate between the primary and secondary antibody responses. Antibody structure & diversity: antibodies, also called immunoglobulins, are members of the larger immunoglobulin superfamily of proteins. Made by the body in response to an antigen, antibodies are the keys to immunological specificity: like miniature smart bombs, antibody immunoglobulins individually circulate through blood, ignoring all antigens except those for which they were designed. Antibody structure: an antibody is a y-shaped structure made up of four polypeptides: Two large heavy chains and two smaller light chains, connected by disulfide bonds. Antibody structure: a typical antibody molecule has two antigen-binding sites, each of which binds identical antigens. This can lead to a phenomenon called immunoprecipitation. Antibodies have constant and variable: an antibody has: Denoted ch and cl, for heavy and light chains. Denoted vh and vl, for heavy and light chains, respectively.

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