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Immunoglobulin

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Arunkumar Durairaj

Antibodies, also known as immunoglobulins, are proteins produced by plasma cells that recognize and bind to specific antigens. There are five classes of antibodies - IgG, IgM, IgA, IgD, and IgE - which have different structures and functions. An antibody molecule is composed of two heavy chains and two light chains that form sites for antigen binding. The variable regions of the heavy and light chains are responsible for binding to different antigens with high specificity.

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Immunoglobulin
Antibodies Proteins that recognize and bind to a particular antigen with very high specificity. Made in response to exposure to the antigen. Each antibody has at least two identical sites that bind antigen: Antigen binding sites.
Antibodies Valence of an antibody: Number of antigen binding sites. Most are bivalent. Belong to a group of serum proteins called immunoglobulins (Igs).
Antibodies or Immunoglobulins * Five classes of Antibodies: IgG IgM IgA IgD IgE
Immunoglobulins
Antibody Structure Immunoglobulins are glycoproteins made up of: - Four polypeptide chains (IgG): a- Two light (L) polypeptide chains b- Two heavy (H) polypeptide chains - The four chains are linked by disulfide bonds - Terminal portion of L-chain contains part of antigen binding site - H-chains are distinct for each of the five Immunoglobulins - Terminal portion of H-chain participate in antigen binding site - The other (Carboxyl) terminal portion forms Fc fragment
Antibody Structure
ANTIBODY STRUCTURE An antibody molecule is composed of two identical Ig heavy chains (H) and two identical light chains (L), each with a variable region (V) & constant region (C).
Variable (V) and Constant (C) Regions - Each H-chain and each L-chain has V-region and C-region - V-region lies in terminal portion of molecule - V-region shows wide variation in amino a. sequences - Responsible for the antigen binding. - C-region lies in carboxyl or terminal portion of molecule - C-region shows an unvarying amino acid sequence - It is responsible for biologic functions
1. Fab region 2. Fc region 3. Heavy chain (blue) with one variable (VH) domain followed by a constant domain (CH1), a hinge region, and two more constant (CH2 and CH3) domains. 4. Light chain (green) with one variable (VL) and one constant (CL) domain 5. Antigen binding site (paratope) 6. Hinge regions.
Immunoglobulin Classes I. IgG Structure: Monomer Percentage serum antibodies: 80% Location: Blood, lymph, intestine Half-life in serum: 23 days Complement Fixation: Yes Placental Transfer: Yes Known Functions: Enhances phagocytosis, neutralizes toxins and viruses, protects fetus and newborn.
Immunoglobulin Classes II. IgM Structure: Pentamer Percentage serum antibodies: 5-10% Location: Blood, lymph, B cell surface (monomer) Half-life in serum: 5 days Complement Fixation: Yes Placental Transfer: No Known Functions: First antibodies produced during an infection. Effective against microbes and agglutinating antigens.
Immunoglobulin Classes III. IgA Structure: Dimer Percentage serum antibodies: 10-15% Location: Secretions (tears, saliva, intestine, milk), blood and lymph. Half-life in serum: 6 days Complement Fixation: No Placental Transfer: No Known Functions: Localized protection of mucosal surfaces. Provides immunity to infant digestive tract.
Immunoglobulin Classes IV. IgD Structure: Monomer Percentage serum antibodies: 0.2% Location: B-cell surface, blood, and lymph Half-life in serum: 3 days Complement Fixation: No Placental Transfer: No Known Functions: In serum function is unknown. On B cell surface, initiate immune response.
Immunoglobulin Classes V. IgE Structure: Monomer Percentage serum antibodies: 0.002% Location: Bound to mast cells and basophils throughout body. Blood. Half-life in serum: 2 days Complement Fixation: No Placental Transfer: No Known Functions: Allergic reactions. Possibly lysis of worms.

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Immunoglobulin

  • 2. Antibodies Proteins that recognize and bind to a particular antigen with very high specificity. Made in response to exposure to the antigen. Each antibody has at least two identical sites that bind antigen: Antigen binding sites.
  • 3. Antibodies Valence of an antibody: Number of antigen binding sites. Most are bivalent. Belong to a group of serum proteins called immunoglobulins (Igs).
  • 4. Antibodies or Immunoglobulins * Five classes of Antibodies: IgG IgM IgA IgD IgE
  • 6. Antibody Structure Immunoglobulins are glycoproteins made up of: - Four polypeptide chains (IgG): a- Two light (L) polypeptide chains b- Two heavy (H) polypeptide chains - The four chains are linked by disulfide bonds - Terminal portion of L-chain contains part of antigen binding site - H-chains are distinct for each of the five Immunoglobulins - Terminal portion of H-chain participate in antigen binding site - The other (Carboxyl) terminal portion forms Fc fragment
  • 8. ANTIBODY STRUCTURE An antibody molecule is composed of two identical Ig heavy chains (H) and two identical light chains (L), each with a variable region (V) & constant region (C).
  • 9. Variable (V) and Constant (C) Regions - Each H-chain and each L-chain has V-region and C-region - V-region lies in terminal portion of molecule - V-region shows wide variation in amino a. sequences - Responsible for the antigen binding. - C-region lies in carboxyl or terminal portion of molecule - C-region shows an unvarying amino acid sequence - It is responsible for biologic functions
  • 10. 1. Fab region 2. Fc region 3. Heavy chain (blue) with one variable (VH) domain followed by a constant domain (CH1), a hinge region, and two more constant (CH2 and CH3) domains. 4. Light chain (green) with one variable (VL) and one constant (CL) domain 5. Antigen binding site (paratope) 6. Hinge regions.
  • 11. Immunoglobulin Classes I. IgG Structure: Monomer Percentage serum antibodies: 80% Location: Blood, lymph, intestine Half-life in serum: 23 days Complement Fixation: Yes Placental Transfer: Yes Known Functions: Enhances phagocytosis, neutralizes toxins and viruses, protects fetus and newborn.
  • 12. Immunoglobulin Classes II. IgM Structure: Pentamer Percentage serum antibodies: 5-10% Location: Blood, lymph, B cell surface (monomer) Half-life in serum: 5 days Complement Fixation: Yes Placental Transfer: No Known Functions: First antibodies produced during an infection. Effective against microbes and agglutinating antigens.
  • 13. Immunoglobulin Classes III. IgA Structure: Dimer Percentage serum antibodies: 10-15% Location: Secretions (tears, saliva, intestine, milk), blood and lymph. Half-life in serum: 6 days Complement Fixation: No Placental Transfer: No Known Functions: Localized protection of mucosal surfaces. Provides immunity to infant digestive tract.
  • 14. Immunoglobulin Classes IV. IgD Structure: Monomer Percentage serum antibodies: 0.2% Location: B-cell surface, blood, and lymph Half-life in serum: 3 days Complement Fixation: No Placental Transfer: No Known Functions: In serum function is unknown. On B cell surface, initiate immune response.
  • 15. Immunoglobulin Classes V. IgE Structure: Monomer Percentage serum antibodies: 0.002% Location: Bound to mast cells and basophils throughout body. Blood. Half-life in serum: 2 days Complement Fixation: No Placental Transfer: No Known Functions: Allergic reactions. Possibly lysis of worms.