10. Describe the physiological roles of the different subclasses of immunoglobulins. How do the structures of these compounds relate to the function of the different classes of immunoglobulins (50 Marks?)
There are four different subclasses of immunoglobulins which are IgM, IgG, IgA and the IgE. Each subclass has its physiological role in relation to its structure. The m immunoglobulin (IgM) is the first primary subclass which is produced due to primary response of the immune system. IgM is the second most dominate and abundant Ig in the serum. IgG is the most abundant in the serum.
The IgM monomer has a structure with two heavy chains which are mu (m) and also two light chains the k and l. The IgM has no hinge region however it has a CH4 …show more content…
It is subdivided into two i.e. the IgA1 and IgA2. Its structure consists of two identical heavy chains of alpha (a) and also two light chains of kappa and lambda. Its structure can be found to form trimers. Only in rare incidences, the structure of IgA forms big polymers. IgA enables the neutralisation so the activities of some viruses inside and also outside the epithelium cells. It also prevents the attachment of the antigens to the gut walls.
The final sub-class of Ig is the E immunoglobulin (IgE). The IgE has been experiments by numerous functional methods. It is mostly induced by the virus. The IgE monomer has sedimentation. Its heavy chains consist of four constant domains (CH). Its structure is bigger than that of the IgG. The structure of the IgE has a fragment which is usually bonded by receptors especially on the mast cells.
The mast cells enable the release of powerful inflammation mediators which are found in the cell granules. IgE makes the immunity strong against diseases. IgE is a very effective defence mechanism against parasitic infections. Vigorous stimulation of the IgE is stimulated by Helminths, which is a parasite-specific antibody in the immune system. IgE has also been posited to play a very crucial role in recognition of foreign materials in the early
There are four different subclasses of immunoglobulins which are IgM, IgG, IgA and the IgE. Each subclass has its physiological role in relation to its structure. The m immunoglobulin (IgM) is the first primary subclass which is produced due to primary response of the immune system. IgM is the second most dominate and abundant Ig in the serum. IgG is the most abundant in the serum.
The IgM monomer has a structure with two heavy chains which are mu (m) and also two light chains the k and l. The IgM has no hinge region however it has a CH4 …show more content…
It is subdivided into two i.e. the IgA1 and IgA2. Its structure consists of two identical heavy chains of alpha (a) and also two light chains of kappa and lambda. Its structure can be found to form trimers. Only in rare incidences, the structure of IgA forms big polymers. IgA enables the neutralisation so the activities of some viruses inside and also outside the epithelium cells. It also prevents the attachment of the antigens to the gut walls.
The final sub-class of Ig is the E immunoglobulin (IgE). The IgE has been experiments by numerous functional methods. It is mostly induced by the virus. The IgE monomer has sedimentation. Its heavy chains consist of four constant domains (CH). Its structure is bigger than that of the IgG. The structure of the IgE has a fragment which is usually bonded by receptors especially on the mast cells.
The mast cells enable the release of powerful inflammation mediators which are found in the cell granules. IgE makes the immunity strong against diseases. IgE is a very effective defence mechanism against parasitic infections. Vigorous stimulation of the IgE is stimulated by Helminths, which is a parasite-specific antibody in the immune system. IgE has also been posited to play a very crucial role in recognition of foreign materials in the early