Immunoglobulin D (IgD) is one of the five classes of immunoglobulins. It is present in small amounts in the body and its specific function is often described as unknown.

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Five Classes of Immunoglobins

Voet, D., Voet, J. G., & Pratt, C. W. (2013). Chapter 7: Protein Function: Myoglobin and Hemoglobin, Muscle Contractions, and Antibodies. In Fundamentals of biochemistry: Life at the molecular level (4th ed., pp. 176-216). Hoboken, NJ: Wiley. Retrieved February 21, 2021, from archive.org.

Fundamental of biochemistry: Life of the molecular level 4th edition: Chapter 7

- Consists of five Y shaped molecules around a J subunit. 
- Most effective against microorganisms
- First immunoglobin released when responding to an antigen. 

- Occurs as monomer, dimer, trimer or a tetramer antibody subunit. 
- Mostly found in the intestinal tract 
- Defense against pathogens by adhering to their antigenic sites and blocks their attachment to outer surfaces. 


IgA 

- Most common immunoglobin 
- It is equally found in the blood and the extravascular fluids 
- It consists of the heavy change and two lighter chains 
- Share the same overall structure, but they are capable of binding different antigens 


- Normally present in the blood in small concentrations 
- Protects against parasites 
- It is connected to the response against allergic reactions


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