1050 Unit 2 Flashcards
what electrophoretic fraction of serum contains the majority of the immunoglobulins?
gamma phase
What are 2 characteristics of an isotype?
-located in the same species
-located in constant region of heavy chains
What are 2 characteristics of an alltoype?
-same species have allotypes present, some do not
-located in constant regions of the IgG subclasses, one IgA subclasses and the gamma light chain
What are 2 characteristics of an idiotype?
-variation in variable regions that give individual antibody molecules specificity
-located in amino acid and terminal region of heavy and light chains
Differentiate between light and heavy chains of immunoglobulins and indicate Greek letter
-heavy chain: (y) gamma, 50,000 d molecular weight, unique to IgG molecules
-light chain: 2 types –> (k) kappa and lambda (upside down y). Molecular weight is 22,000 d. found is all subclasses but only one type is present in a single molecule.
Discuss the effects of treating an immunoglobulin with papain
One or more peptide bonds in the hinge region are split. Producing 3 fragments -two Fab fragments and on Fc fragments
Discuss the effects of treating an immunoglobulin with pepsin
- cleaves the Ig above the set of disulfide bond that hold together the H chains.
-F(ab)2 created (contains 2 antigen binding sites)
-Fc portion (in nonfunctional pieces
Describe characteristics of IgG ( half life, molecular weight, amount, Greek letter)
- most abundant in serum (70-75%)
- gamma (y)
-longest half life at 23 days - monomer w/ molecular weight of 150,000 d
-4 subclasses: IgG1 (66%), IgG2 (23%), IgG3 (7%) and IgG4 (4%)
-increases with second exposure
-lab testing: precipitation and agglutination
What are the functions of IgG?
-neutralizes toxins and bacteria
-binds complement
-binds to receptors on phagocytic cells
-able to cross over to placenta
Describe characteristics of IgM (half life, molecular weight, amount in serum, Greek letter)
-muu (u) Greek letter
-“macroglobulin”
-pentamer with 10 antibody-binding sites. can also exist as a monomer
-indicates acute infection
-molecular weight of 900,000 d
-accounts for 5-10%
- half life of 6 days
-contains a J chain (joining). Forms disulfide bonds.
What are the functions of IgM?
-neutralizes toxins and bacteria
-primary antibody response
-binds efficiently to complement (complement fixation)
-causes efficient agglutination of antigens
Describe characteristics of IgA
- accounts for 10-15%
-half life of 5 days - alpha (a)
-molecular weight of 160,000 d
-monomer in serum, dimer in secretion
-2 sub classes and secretory IgA
-present in breast milk
What are the functions of IgA?
-pass immunity through breast milk
-protects mucosal surfaces and prevents bacteria adherence.
-neutralizes toxins produced by microorganisms
-acts as opsonin’s
-act as anti-inflammatory (IgA1)
Describe characteristics of IgD
-appears second, after IgM
-molecular weight is 180,000 d
-only accounts for 0.001% (rare)
half life of 1-3 days
- sigma (s)
-most susceptible to protelysis
-has extended hinge region
What are the functions of IgD?
-present as an antigen receptor on B cells (immunocompetent but unstimulated B-cells)
-role in B cell activation
-identifies mature B cells.
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Describe characteristics of IgE
-half life of 2-3 days
-accounts for 0.005%
molecular weight of 190,000 d
-heavy chain with 4 constant regions
-(E) Greek letter?
What are the functions of IgE?
-binds to mast cells, basophils and eosinophils.
-triggers allergic reaction
-role is response to parasites, binding to eosinophils that release enzymes that kill large antigens (parasites)
-2 adjacent IgE molecules on mast cells bind a specific antigen
results in degranulation of mast cells and release of vasoactive amines (histamine and heparin)
what are some characteristics of IgG2, IgG3, and IgG4?
-IgG3–>most efficient binding complement. Induced in response to antigen proteins
-IgG2 and IgG4–> poor mediators of complement activation. involved in response to polysaccharides antigen
Describe IgA1 and IgA2
-IgA1–> acts as anti-inflammatory by downregulating IgG mediated phagocytosis, chemotaxis, bactericidal activity, and cytokine release
-IgA2–> found is secretion of mucosal surfaces (respiratory, urogenital and intestinal tract)
Describe and give characteristics of Secretory IgA
-synthesized by plasma cells
-released as a dimer held together by a J chain
-contains secretory complement (SC) derived from epithelial cells
-neutrophils, macrophages and monocytes posses specific receptors
-binding triggers respiratory burst and degranulation of cells is involved
Describe functions of the J chain and the secretory component and indicate which immunoglobulin class they are found in
- j chain–> joining
-glycoprotein that holds together monomeric units in IgM, the residue forms disulfide bonds.
-holds together 2 monomers in IgA. Essential for polymerization and secretion of IgA.
-Secretory complement–> present in IgA. derived from epithelial cells found in close proximity of plasma cells. serves as specific receptor for IgA
Discuss how IgD is different from the other types
- most susceptible to proteolysis
-does not provide protection
What type of cells do the IgE bind to in an allergic reaction?
-mast cells, basophils, and activated eosinophils
Compare and contrast the primary and secondary antibody response to an antigen
-primary –> long lag phase (4-7 days), low antibody titer (lowers in few days), low affinity for antigen
-secondary–> IgM produced, followed by a greater predominance of IgG, higher IgG titer which declines slowly over a long period of time, high affinity for antigen