Related Experiment Video

Updated: Aug 12, 2026

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
11:10

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

The monocyte binding domain(s) on human immunoglobulin G

J M Woof, M I Nik Jaafar, R Jefferis

    Molecular Immunology
    |June 1, 1984
    PubMed

    Monocyte binding has previously been assigned to the C gamma 3 domain of human immunoglobulin G (IgG) largely on the ability of the pFc' fragment to inhibit the monocyte-IgG interaction. This ability is markedly reduced compared to the intact parent IgG. We find this result with a conventional pFc' preparation but this preparation is found to contain trace contamination of parent IgG as demonstrated by reactivity with monoclonal antibodies directed against C gamma 2 domain and light-chain epitopes of human IgG. Extensive immunoaffinity purification of the pFc' preparation removes its inhibitory ability indicating that this originates in the trace contamination of parent IgG (or Fc). Neither of the human IgG1 paraproteins TIM, lacking the C gamma 2 domain, or SIZ, lacking the C gamma 3 domain, are found to inhibit the monocyte-IgG interaction. The hinge-deleted IgG1 Dob protein shows little or no inhibitory ability. Indirect evidence for the involvement of the C gamma 2 domain in monocyte binding is considered. We suggest finally that the site of interaction is found either on the C gamma 2 domain alone or between the C gamma 2 and C gamma 3 domains.

    More Related Videos

    Use of a Monocyte Monolayer Assay to Evaluate Fcγ Receptor-mediated Phagocytosis06:27

    Use of a Monocyte Monolayer Assay to Evaluate Fcγ Receptor-mediated Phagocytosis

    Published on: January 2, 2017

    Characterization of Human Monocyte Subsets by Whole Blood Flow Cytometry Analysis09:12

    Characterization of Human Monocyte Subsets by Whole Blood Flow Cytometry Analysis

    Published on: October 17, 2018

    Related Concept Videos

    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...
    Transcytosis of IgG01:15

    Transcytosis of IgG

    Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
    IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
    Immunoglobulin-like Cell Adhesion Molecules01:31

    Immunoglobulin-like Cell Adhesion Molecules

    Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
    Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
    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.
    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...