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01:15Western Blotting
Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
01:33Enzyme-Linked Immunosorbent Assay
In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
01:28Protein Denaturation
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
01:27SDS-PAGE
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
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Immunological reactions between films of antigen and antibody molecules.
The Journal of biological chemistry·2010
Related Experiment Video
Updated: Jun 19, 2026
08:38
Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
Published on: August 14, 2011
SEROLOGICAL REACTIONS OF PROTEIN FILMS AND DENATURED PROTEINS.
1Laboratories of The Rockefeller Institute for Medical Research.
The Journal of Experimental Medicine
|October 30, 2009
Summary
Protein films bind specifically with antibodies, demonstrating that reactions occur regardless of molecular structure. This research highlights the potential for antigen-antibody reactions in various biological contexts.
Area of Science:
- Immunochemistry
- Biochemistry
- Protein Science
Background:
- Antibody-antigen interactions are crucial in immunology.
- The role of protein structure in these specific binding reactions requires further elucidation.
Purpose of the Study:
- To investigate if protein films can specifically combine with antibodies.
- To determine if these reactions are independent of the protein's native compact structure.
- To explore species-specific antigen-antibody reactions using protein films.
Main Methods:
- Preparation of protein films (hen ovalbumin, serum albumins, globulins).
- Exposure of protein films to specific antibodies (antisera).
- Observation of specific binding and reactivity.
Main Results:
- Proteins in film form (ovalbumin, albumins, globulins) specifically combined with antibodies.
- Reactions occurred independently of the protein's compact molecular structure.
- Serum globulin films lost reactivity over time on the water surface.
- Species-specific reactions were confirmed for serum albumin films and in precipitin tests.
- Specific antibody fixation was observed with pneumococcal polysaccharides.
Conclusions:
- Protein films retain specific antigen-antibody binding capabilities.
- The compact structure of proteins is not essential for specific antibody recognition.
- Protein film assays offer a valuable method for studying antigen-antibody interactions and specificity.