Campbell Biology (10th Edition)
Campbell Biology (10th Edition)
10th Edition
ISBN: 9780321775658
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 43, Problem 8TYU
Summary Introduction

To draw: The antibody-linking protein complex that could trigger endocytosis by a macrophage.

Introduction: An antigen is a large molecule. It may be made up of proteins or polysaccharides. A single antigen has several binding sites that are called epitopes. Each antibody binds to a specific epitope of an antigen. An antibody is a Y-shaped protein molecule that consists of four polypeptide chains. There are two identical heavy chains and two identical light chains connected by a disulfide bond. Antibody binds to the antigen receptor of pathogens like bacteria or virus.

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Consider a pencil-shaped protein with two epitopes, Y (the “eraser” end) and Z (the “point” end). They are recognized by antibodies A1 and A2, respectively. Draw and label a picture showing the antibodies linking proteins into a complex that could trigger endocytosis by a macrophage.
How are antibodies unique? Please discuss the structure of an antibody. What are the V and C regions? Discuss how the few hundred genes involved are capable of making endless amounts of antibodies. Besides medical treatment what is another way antibodies can be used?
For the diagram below, all of the following statements are true EXCEPT: Antigen- binding site V C Heavy chain V Light chain S.S. Fc (stem) region c C Hinge region None of the other four answers (All are true statements) Antibodies (Immunoglobulins) are composed of four protein molecules, two identical "light" chains and two identical "heavy" chains Antigens bind to the "stem", composed of the constant regions of the two "heavy" chains The variable (V) regions form the antigen binding sites The constant (C) regions determine class of antibody
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