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Which of the following is NOT true about antibodies a. an antibody has more than one antigen binding site b. a pathogen can have different epitopes c. a pathogen makes more than one antigen?
Wiki User
∙ 11y ago
C is false.
A pathogen can have multiple epitopes and antigens. A single antigen is simply one molecule, and the cell surface is littered with millions of antigens.
Wiki User
∙ 11y ago
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Does o blood type have a antigens?
Has no antigen in many textbooks it will state "no A-antigen and no B-antigen"(which imply the possibility of some other antigen) and some will even say, "no antigen" (which is true; antigens are things that attach to antigen binding sites, thus, if it does not fit any antigen binding sites, it is technically not a antigen but merely a "enzyme/protein") but this is just to reduce unnecessary and irrelevant information; they are only concerned about A-antibody, B-antibody, A-antigen, and B-antigen. Nonetheless, know that there are in fact antigens on o blood cells, they are just inactive. My guess is, N acetyl glactosamine on A antigen and Galactose on B antigens are Epitopes (: a small specific regions on antigens that are bound by the antigen receptors on lymphocytes and by secreted antibodies.) Antigens without epitopes will not be detected by antigen binding sites.
What is linked recognition?
Linked Recognition occurs when a B cell is activated by a helper T cell that responds to the same antigen as the B cell. The epitope recognized by the B cell must be "linked" to the epitope recognized by the helper T cell--in a manner such that both epitopes are physically linked in a certain manner. However, the two epitopes need not be the same. The importance of linked recognition can be observed in maintaining self tolerance. Also, a B cell recognized by a helper T cell is up to 10,000 times more efficient at displaying peptide fragments on their MHC class II molecures than B cells that are not helped.
Which portions of an antibody bind to the epitopes?
paratopes
What region of an antibody does the antigen bind to?
epitopes on the antigen while the paratopes on the antibody
Why polyclonal antibody tend to have cross-reaction compare to monoclonal antibody?
Polyclonal antibody recognizes several epitopes on the target protein while monoclonal antibody recognizes only single epitope, hence monoclonal antibodies are more specific than polyclonal antibodies. However, sometimes MAbs are not able to precipitate the antigen because the epitope might need to be exposed on the surface of the antigen to be recognized by the antibody. Since some of the epitope might be hidden and it's a single epitope that is recognized by the monoclonal antibody, the propability of the antibody to reconize the epitope is lower compared with the polyclonal antibody that recognizes several epitopes on the target protein this is the reason for the tendency of polyclonal antibodies to have cross-reaction as compared to MAbs. by Victor S Gruezo Jr
Why is it important that the capture and detection antibodies recognize different epitopes in ELISA?
Capture and detection antibodies must recognise two non-overlapping apitopes in order to work. Once the detection antibody is bound, the capture antibody cannot obscure the epitope used by the detection antibody in any way, or the sandwich ELISA will not work. Hope that helps, I am also trying to answer a similar question and this is what i have found out so far, but not 100% sure that its right. Eve
Why polyclonal antibody solution is able to precipitate its antigen protein whereas monlclonal antibody solution has hard time to do so?
Polyclonal antibody recognizes several epitopes on the target protein while monoclonal antibody recognizes only single epitope. Sometimes, monoclonal antibodies are not able to precipitate the antigen because the epitope might need to be exposed on the surface of the antigen to be recognized by the antibody. Since the epitope might be hidden and it's a single epitope that is recognized by the monoclonal antibody, the propability of the antibody to reconize the epitope is lower compared with the polyclonal antibody that recognizes several epitopes on the target protein.
How do macrophages recognize infectious agents such as bacteria?
When antibodies bind to the epitopes of an antigen(bacteria) via antigen receptors, the antibodies present the bacteria to a macrophages in a form that they recognize the foreign substance and engulf them. This antibody-antigen "team work" is also known as opsonization
How do you rise antibody for specific substance?
it can be rised according to the epitopes present in antigen that enters our body..if separate antibody is rised to each specific epitope v call it as monoclonal antibody
Definition of epitope?
part of an antigen moleculle inside our body. Example: antibody are bound because of epitopes.
Define and distinguish antibody affinity and avidity?
An antibody (IgM for example is a pentamere), can consist out of more than one different immonoglobulines. One of the variabel regions of these immunoglobulines can bind to an epitope of an antigene, this is called affinity. When different variabel regions of one antibody bind to different epitopes on an antigene, the combined effect is called avidity. The effect is not equal to the sum of the affinity's.
What are blood antibodies?
Antibodies are cells that are made in the body. They are involved in immunity. Any foreign invader (antigen) that enters the body will be engulfed by its corresponding antibody, if that antibody is present in the body.
What is an antibody and what do?
Antibodies (also known as immunoglobulins,abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
What does antibodies mean?
Antibodies (also known as immunoglobulins,abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
