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Primary Reference: Cellular and Molecular Immunology, 8th ED. Statement 1 is only part true. B cells produce b cell receptors of a specific paratope, that are randomly determined during maturation. The process of V(d)j recombination, where productive rearrangements in the heavy chain and light chain genes, produces a primary CHtranscript consisting of ...


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Statement 1 is true. Statement 2 is false. My explanation is from the perspective of immune cell development: The antibody-producing B cells are called plasma B cells. Plasma B cells are differentiated from a single naïve B cell (undifferentiated B cell). The naïve B cell have all the cell structure. However, naïve B cell can also be differentiated into ...


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Statement 1 is true and Statement 2, false. B cells, in the absence of antigenic stimulation express surface receptors(B-cell receptors or BCRs), which look like normal secreted antibodies (but these are membrane bound and not secreted). What is amazing is that each B cell at a particular time expresses the same B cell receptor - same as in, all receptors ...


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The letter suffix in the name or abbreviation of an immunoglobulin specifies which type of "heavy chain" the immunoglobin contains. The heavy chain is the large polypeptide (amino acid chain) found in the antibody. In mammals there are five different classes or types of heavy chains, and these types are given Greek letters to differentiate them. As ...


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The problem is partly the definition of Antigen that you quote. It refers to “the body” leading you to assume it’s a specific body — yours. I'm sure there are better definitions, but just taking this one, I would modify to: “A substance that can be recognised as foreign and evoke an immune response in an organism.” With this definition, which is actually ...


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I’m not an immunologist, but I think it fair to say that antibodies may well be able to bind to certain food or drugs. However there are several reasons that this may not cause their removal or trigger an immune response. These include: Location. If the food is in the stomach I imagine that the digestive environment favours breakdown to sugars, amino acids ...


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I want to add something on top of Chris answer. The production of an antibody it is usually a quite slow (and expensive) process, an alternative that worth to consider is phage display (https://en.wikipedia.org/wiki/Phage_display). Once you find the phage that effectively bind your protein of interest, you can use it instead of an antibody in what is called ...


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I think the most promising routes use antibodies. You could either develop an ELISA or do western blot analysis of plant material - both need a good and specific antibody. To generate these, the protein of interest (or at least parts of it) are injected into animals (typically mice or rabbit) and then antibodies are pourified from the blood of these animals. ...



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