Related Experiment Video
Updated: Jun 19, 2026
13:53
Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
Published on: December 19, 2020
THE ANTIGENIC PROPERTIES OF SPLIT PRODUCTS OF CASEIN.
1Hearst Laboratory of Pathology and Bacteriology, and the Rudolph Spreckels Physiological Laboratory of the University of California, Berkeley.
The Journal of Experimental Medicine
|October 30, 2009
Summary
Casein and paranuclein exhibit distinct antigenic properties, with casein more readily inducing specific antibodies. Split products lack significant antigenic activity, indicating protein structure is key to immune response.
Area of Science:
- Immunology
- Biochemistry
- Protein Chemistry
Background:
- Understanding the antigenic properties of proteins is crucial for immunology and allergy research.
- Casein, a major milk protein, and its derivatives are common allergens.
- Previous studies have explored protein antigenicity, but a systematic analysis of purified casein split products was needed.
Purpose of the Study:
- To investigate the distinct antigenic properties of chemically pure casein and its split products.
- To determine the specificity of antibodies generated against casein and paranuclein.
- To assess the antigenic potential of casein's peptic digestion products and constituent amino acids.
Main Methods:
- Sensitization of guinea pigs to induce anaphylaxis.
- Immunization of rabbits with casein and paranuclein.
- Testing of antisera for precipitins and complement fixation antibodies.
- Evaluation of peptic digest products and amino acids for antigenic activity.
Main Results:
- Casein and paranuclein demonstrated distinct antigenic properties, capable of sensitizing guinea pigs.
- Casein immunization produced specific antibodies more readily than paranuclein.
- Complete peptic digestion products and key amino acids (glutamic acid, leucine) showed no significant antigenic properties.
- Antibodies to casein were quantitatively specific, while antibodies to paranuclein were absolutely specific.
Conclusions:
- The structural integrity of casein is essential for its potent antigenic properties.
- Specific regions or structures within the intact protein molecule are likely responsible for antigenicity.
- Split products of casein, including amino acids, do not elicit a significant immune response, highlighting the importance of protein conformation.
More Related Videos
Related Concept Videos
01:26Antigens Involved in Adaptive Immunity
An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
00:42Cross-reactivity
Overview
01:10Antibody Structure
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
01:25Antibody Structure and Classes
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
01:26Antibody Actions
Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
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.