Biochemistry Chapter: Immunoglobulins

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Where are carbohydrates usually attached to in most immunoglobulins?

CH2 domain

What is the basis of classification of human immunoglobulins into five classes?

Heavy chains

Which immunoglobulin exists as a monomer, dimer, or pentamer?

IgA

What is the primary function of IgE?

<p>Mediation of allergic response</p> Signup and view all the answers

Which immunoglobulin is responsible for transplacental passage?

<p>IgG</p> Signup and view all the answers

What is the function of IgD?

<p>B-cell activation</p> Signup and view all the answers

Which immunoglobulin has the highest serum concentration?

<p>IgG</p> Signup and view all the answers

What is the primary function of IgA?

<p>Protection of mucosal tissues</p> Signup and view all the answers

Which type of cells produce immunoglobulins?

<p>Plasma cells</p> Signup and view all the answers

What type of bonds link the heavy and light chains together in immunoglobulins?

<p>Disulfide bonds</p> Signup and view all the answers

In immunoglobulins, what does the 'VL' region stand for?

<p>Variable Light</p> Signup and view all the answers

The hinge region of an antibody provides which characteristic?

<p>Flexibility</p> Signup and view all the answers

What is the molar mass range of the heavy chains in immunoglobulins?

<p>53-75 kDa</p> Signup and view all the answers

Which of the following regions are found in a light chain of immunoglobulins?

<p>VL and CL</p> Signup and view all the answers

What are the functions of immunoglobulins?

<p>Binding and destroying specific antigens</p> Signup and view all the answers

Which regions based on amino acid sequences variability are found in the heavy chain of immunoglobulins?

<p>VH and CH</p> Signup and view all the answers

Study Notes

Immunoglobulins

  • Immunoglobulins are glycoprotein molecules produced by plasma cells, a critical component of the immune response.
  • They recognize, bind, and destroy specific antigens such as bacteria or viruses.
  • Immunoglobulins function as antibodies.

Structure of Immunoglobulins

  • Each immunoglobulin has a 4-chain structure consisting of 2 identical heavy chains (53-75 kDa) and 2 identical light chains (23 kDa).
  • Heavy and light chains are linked together by disulfide bonds.
  • Disulfide bonds include inter-chain disulfide bonds (between polypeptide chains) and intra-chain disulfide bonds (within polypeptide chains).

Regions of Immunoglobulins

  • Variable (V) regions: VL (Variable Light) and VH (Variable Heavy) with variable amino acid sequences.
  • Constant (C) regions: CL (Constant Light) and CH (Constant Heavy) with constant amino acid sequences.

Domains of Immunoglobulins

  • Light Chain Domains: VL and CL.
  • Heavy Chain Domains: VH, CH1 to CH3 (or CH4).

Hinge Region

  • The hinge region is where the arms of the antibody molecule form a Y, allowing for flexibility in the molecule.

Types of Immunoglobulins

  • IgA, IgD, IgE, IgG, and IgM.
  • IgG: monomer, 75% serum, 1000 serum concentration.
  • IgA: monomer or dimer, 15% serum, 200 serum concentration.
  • IgM: pentamer, 9% serum, 120 serum concentration.
  • IgD: monomer, 0.2% serum, 3 serum concentration.
  • IgE: monomer, 0.04% serum, 0.05 serum concentration.

Functions of Immunoglobulins

  • Ag binding: binds to specific antigenic determinants, protecting the host.
  • Effector functions: fixation of complement, opsonization of bacteria, and binding to various cells.

Major Functions of Immunoglobulins

  • Complement fixation: IgG, IgM.
  • Transplacental passage: IgG.
  • Mediation of allergic response: IgE.
  • Protection of mucosal tissues: IgA.
  • Opsonization: IgG.
  • B-cell activation: IgD.
  • Ag receptor on B-cell: IgM.

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