By Dortort F.
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Extra resources for Conophytum
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Chapter 4 Preparation of Immunogens and Production of Antibodies Hei-ti Hsu, Tsung-chi Chen, Chin-an Chang, and Shyi-dong Yeh Summary The quality of reagents greatly affects the interpretation of serological tests. Methods used in conventional viral purification and molecular cloning and expression of target viral proteins to obtain antigens for immunization are presented. Immunization of rabbits, mice and chickens and isolation of immunoglobulin from immunized animals also are described. Key words: Antibody, Antigen, IgG, IgY, Immunization, Immunoglobulin isolation, Protein expression.
Quinoa plants are inoculated at 8–10 leaf stage and kept in a greenhouse at 25–30°C (see Note 1). 2. 1% cysteine. 3. Cheese cloth or Miracloth. 4. 01 M glycine. 5. 35% Cesium sulfate in TBG buffer. 6. Triton X-100. 7. Beckman high speed JA41, ultracentrifuge SW 41, 35 Ti and 60 Ti rotors. 8. Protein dissociation buffer. 9. 25 M KCl. 2. E. coli Expression Traditionally, virions purified from infected tissue are used as immunogen to prepare diagnostic polyclonal antiserum. However, not every virus is easily purified from infected tissue.
Antibodies produced by this route are always immunoglobulin class M as only one immunisation is used. This method is covered by Animal Procedures legislation in most countries as it is an invasive surgical procedure and welfare issues must be addressed. The antigen must be in a highly aggregated or immobilised form. This technique is frequently used to produce antibodies to proteins separated by electrophoresis. The gel is stained in the normal manner and the proteins blotted over onto nitrocellulose.