Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Antibody Structure and Classes01:25

Antibody 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.
Polymers: Defining Molecular Weight01:01

Polymers: Defining Molecular Weight

Unlike small molecules with definite molecular weights, polymers are a mixture of individual polymer chains of varying lengths, each with a unique molecular weight. So, the molecular weight of a polymer is expressed as an average value based on the average size of the polymer chains. The two most common forms of averages used for polymers are the number average molecular weight and weight average molecular weight.
The number average molecular weight (Mn) is the summation of the number...
Antibody Structure01:10

Antibody 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...
Antibody Structure01:10

Antibody 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...
Determination of Molar Masses of Polymers II01:27

Determination of Molar Masses of Polymers II

Polymer samples typically consist of macromolecular chains with a distribution of lengths, resulting in a range of molar masses rather than a single discrete value. Conventional descriptors such as the number-average molar mass and weight-average molar mass quantify this distribution but do not fully capture polymer behavior in solution..The viscosity-average molar mass provides a more realistic description of polymer behavior in solution because it accounts for the enhanced contribution of...
Antibody Actions01:26

Antibody 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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Binding of calcium to serum albumin. III. Influence of ionic strength and ionic medium.

Scandinavian journal of clinical and laboratory investigation·2011
Same author

The Protective or Curative Element in Type B H. influenzae Rabbit Serum.

The Yale journal of biology and medicine·2011
Same author

Antibody formation in the immunization of human beings.

Federation proceedings·2010
Same author

Spectrophotometric standardization of complement for fixation tests.

Journal of immunology (Baltimore, Md. : 1950)·2010
Same author

Studies in human malaria; attempts to influence relapsing vivax malaria by treatment of patients with vaccine (Pl. vivax).

Journal of immunology (Baltimore, Md. : 1950)·2010
Same author

Studies in human malaria; an attempt at vaccination of paretics against blood-borne infection with Pl. vivax.

Journal of immunology (Baltimore, Md. : 1950)·2010

Related Experiment Video

Updated: Jun 19, 2026

An Open-Source Framework for Mass Calculation of Antibody-Based Therapeutic Molecules
04:24

An Open-Source Framework for Mass Calculation of Antibody-Based Therapeutic Molecules

Published on: June 16, 2023

THE MOLECULAR WEIGHT OF ANTIBODIES.

M Heidelberger1, K O Pedersen

  • 1Institute of Physical Chemistry, University of Upsala, Upsala, Sweden, and the Department of Medicine, College of Physicians and Surgeons, Columbia University, and the Presbyterian Hospital, New York.

The Journal of Experimental Medicine
|October 30, 2009
PubMed
Summary
This summary is machine-generated.

Rabbit and horse pneumococcus antibodies exhibit distinct molecular characteristics. Ultracentrifuge analysis reveals differences in molecular weight and homogeneity, impacting antibody structure and function.

More Related Videos

Rapid Determination of Antibody-Antigen Affinity by Mass Photometry
10:17

Rapid Determination of Antibody-Antigen Affinity by Mass Photometry

Published on: February 8, 2021

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)
10:00

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)

Published on: June 20, 2019

Related Experiment Videos

Last Updated: Jun 19, 2026

An Open-Source Framework for Mass Calculation of Antibody-Based Therapeutic Molecules
04:24

An Open-Source Framework for Mass Calculation of Antibody-Based Therapeutic Molecules

Published on: June 16, 2023

Rapid Determination of Antibody-Antigen Affinity by Mass Photometry
10:17

Rapid Determination of Antibody-Antigen Affinity by Mass Photometry

Published on: February 8, 2021

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)
10:00

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)

Published on: June 20, 2019

Area of Science:

  • Immunology
  • Biochemistry
  • Protein Chemistry

Background:

  • Antibodies are crucial for immune response.
  • Understanding antibody structure is key to their function.
  • Pneumococcus antibodies provide a model for studying immune proteins.

Purpose of the Study:

  • To investigate the molecular properties of pneumococcus antibodies in different species.
  • To compare the homogeneity and molecular weight of antibodies from rabbits and horses.
  • To analyze the molecular species in specific precipitates of egg albumin and anti-egg albumin.

Main Methods:

  • Ultracentrifugation was used to assess homogeneity and sedimentation constants.
  • Purification of rabbit and horse pneumococcus anticarbohydrates.
  • Analysis of egg albumin-anti-egg albumin specific precipitates.

Main Results:

  • Rabbit Type III pneumococcus anticarbohydrate was homogeneous with a molecular weight similar to normal rabbit globulin (approx. 150,000).
  • Horse Type I pneumococcus anticarbohydrate showed variable homogeneity and a sedimentation constant suggesting a molecular weight 3-4 times that of normal horse globulin.
  • Ultracentrifuge studies on egg albumin-anti-egg albumin precipitates provided insights into molecular interactions.

Conclusions:

  • Significant differences exist in the molecular characteristics of pneumococcus antibodies between rabbits and horses.
  • These molecular variations may influence antibody efficacy and immune response.
  • Further research is needed to fully elucidate the implications of these findings.