Immunoglobulin classes slideshare

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See our User Agreement and Privacy Policy. See our Privacy Policy and User Agreement for details. Published on Apr 29, General structure, classification, function and significance.

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Immunoglobulins- Structure and function. Upcoming SlideShare. Like this presentation? Why not share! Embed Size px. Start on. Show related SlideShares at end. WordPress Shortcode. Namrata Chhabra Follow. Published in: Education. Full Name Comment goes here. Are you sure you want to Yes No. Show More. No Downloads. Views Total views. Actions Shares.

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No notes for slide. Immunoglobulins- Structure and function 1. Immunoglobulins Namrata Chhabra 2. Types of immunity 6. Immunoglobulins The immunoglobulins derive their name from the finding that they migrate in the region of globulins when antibody- containing serum is placed in an electrical field.

Structural characteristics A. Interchain disulphide bonds Interchain disulphide bonds Basic structure of immunoglobulins Fab Digestion with papain breaks the immunoglobulin molecule in the hinge region before the H-H inter-chain disulfide bond. This results in the formation of two identical fragments that contain the light chain and the VH and CH1 domains of the heavy chain.

immunoglobulin classes slideshare

Fc Digestion with papain also produces a fragment that contains the remainder of the two heavy chains each containing a CH2 and CH3 domain.Slideshare uses cookies to improve functionality and performance, and to provide you with relevant advertising. If you continue browsing the site, you agree to the use of cookies on this website. See our User Agreement and Privacy Policy.

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Views Total views. Actions Shares. No notes for slide. Immunoglobulins 1. Immunoglobulins Dr. Pendru Raghunath 2. Immunoglobulin Immunoglobulin is a glycoprotein that is made in response to an antigen and can recognize and bind to the antigen that caused its production.

Each heavy and light chain contains amino terminal in variable region carboxy terminal in constant region 5. Other fragment called Fc fragment Fraction crystallizable 7.Slideshare uses cookies to improve functionality and performance, and to provide you with relevant advertising. If you continue browsing the site, you agree to the use of cookies on this website. See our User Agreement and Privacy Policy. See our Privacy Policy and User Agreement for details. Published on Jul 20, SlideShare Explore Search You.

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We use your LinkedIn profile and activity data to personalize ads and to show you more relevant ads. You can change your ad preferences anytime. What is an Antibody?

immunoglobulin classes slideshare

Immunoglobulins: Classes and Sub classes. Upcoming SlideShare.

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Immunoglobulin Structure and Classes

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Published on Dec 20, This topic covers the brief introduction of Ag and Ab in detail. Types and functions of Ig is explained in detail. Paraproteinemias is explained with simple pictures. Sivaranjani, MD. SlideShare Explore Search You. Submit Search. Home Explore. Successfully reported this slideshow. We use your LinkedIn profile and activity data to personalize ads and to show you more relevant ads. You can change your ad preferences anytime.

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Antibody class switch ppt.

immunoglobulin classes slideshare

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Antibody class switch ppt 1. Antibody Class Switching.

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Presentation by: Gidwani Manish N. Roll No. What Is Ab Class Switching? Instead, the antibody retains affinity for the same antigens, but can interact with different effector molecules.

Antibody Gene Arrangement. Ab Gene Arrangement Contd.This page introduces the nomenclature and criteria used to describe the structure, classes and functional types of immunoglobulins. Antibody or immunoglobulin molecules are glycoproteins composed of one or more units, each containing four polypeptide chains: two identical heavy chains H and two identical light chains L.

The amino terminal ends of the polypeptide chains show considerable variation in amino acid composition and are referred to as the variable V regions to distinguish them from the relatively constant C regions. Heavy and light chains are held together by a combination of non-covalent interactions and covalent interchain disulfide bonds, forming a bilaterally symmetric structure.

The V regions of H and L chains comprise the antigen-binding sites of the immunoglobulin Ig molecules. Each Ig monomer contains two antigen-binding sites and is said to be bivalent. The hinge region is the area of the H chains between the first and second C region domains and is held together by disulfide bonds.

These are distinguished by the type of heavy chain found in the molecule. Differences in heavy chain polypeptides allow these immunoglobulins to function in different types of immune responses and at particular stages of the immune response.

The polypeptide protein sequences responsible for these differences are found primarily in the Fc fragment. Antibody classes differ in valency as a result of different numbers of Y-like units monomers that join to form the complete protein. For example, in humans, functioning IgM antibodies have five Y-shaped units pentamer containing a total of 10 light chains, 10 heavy chains and 10 antigen-binding.

In addition to the major immunoglobulin classes, several Ig subclasses exist in all members of a particular animal species.

Antibodies are classified into subclasses based on minor differences in the heavy chain type of each Ig class. Variance among different subclasses is less than the variance among different classes.

Consequently, antibody-binding proteins e. Antibodies whatever their class or subclass are produced and purified in two basic forms for use as reagents in immunoassays: polyclonal and monoclonal. Typically, the immunological response to an antigen is heterogeneous, resulting in many different cell lines of B-lymphocytes precursors of plasma cells producing antibodies to the same antigen.

All of these cells originate from common stem cells, yet each develops the individual capacity to make an antibody that recognizes a particular determinant epitope on the same antigen.

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Because it contains this heterogeneous collection of antigen-binding immunoglobulins, an antibody purified from such a sample is called a polyclonal antibody. Polyclonal antibodies, which are generally purified directly from serum, are especially useful as labeled secondary antibodies in immunoassays.Slideshare uses cookies to improve functionality and performance, and to provide you with relevant advertising. If you continue browsing the site, you agree to the use of cookies on this website.

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You can change your ad preferences anytime. Immunoglobulin structure and function. Upcoming SlideShare. Like this presentation? Why not share! Embed Size px. Start on. Show related SlideShares at end. WordPress Shortcode. Full Name Comment goes here. Are you sure you want to Yes No. Show More.