OCR · A-Level · Biology

    Course version: H420 · Version from Sept 2025

    (h) the structure and general functions of antibodies

    Full specification wording

    Communicable diseases, disease prevention and the immune system: (h) the structure and general functions of antibodies

    Antibodies are globular glycoproteins of the immunoglobulin family, secreted by plasma cells (differentiated B lymphocytes) in response to a specific antigen.

    Checked against the OCR H420 specification (opens in a new tab) on .

    • Point 8 of 14
    • 4 key terms

    Study notes

    From the checked teaching notes for this specification point.

    The idea

    Antibodies are globular glycoproteins of the immunoglobulin family, secreted by plasma cells (differentiated B lymphocytes) in response to a specific antigen. Each antibody is a Y-shaped molecule of four polypeptide chains: two identical heavy chains and two identical light chains, held by disulfide bridges. The variable regions at the tips of the two arms form the antigen-binding sites, giving each antibody two identical binding sites and a shape complementary to one specific antigen. The constant regions are the same within a class and allow recognition by phagocytes and complement. General functions: binding to antigen to neutralise pathogens or toxins, marking them for destruction, and forming antigen–antibody complexes that can be destroyed by phagocytosis. Binding is specific and reversible.

    What earns the marks

    • Antibodies are proteins (globular glycoproteins/immunoglobulins) secreted by plasma cells derived from B lymphocytes.
    • Each antibody has four polypeptide chains: two heavy and two light chains, joined by disulfide bridges.
    • The Y-shaped molecule has two variable regions forming two identical antigen-binding sites.
    • The binding site shape is complementary to a specific antigen, so binding is specific.
    • Constant regions are the same within a class and allow recognition by phagocytes/complement.
    • General functions include neutralising pathogens or toxins, marking antigens for destruction and forming complexes removed by phagocytosis.

    Common mistakes and how to put them right

    • Saying antibodies are produced by phagocytes or T cells.

      Put it right: Correct that they are secreted by plasma cells (from B lymphocytes).

    • Describing the binding site as complementary to the antibody rather than to the antigen.

      Put it right: Correct that the variable region is complementary to a specific antigen.

    • Claiming antibodies directly kill pathogens.

      Put it right: Correct that they bind, neutralise and mark antigens for destruction by phagocytosis or complement.

    Exam tips

    • Learn the four-chain Y structure with two heavy and two light chains and label the variable and constant regions.
    • Always link structure to function: variable region gives specificity, constant region gives recognition by phagocytes.
    • Use the term 'complementary' when describing antigen–antibody binding rather than 'matching' loosely.

    Try the lesson

    The start of the Communicable diseases, disease prevention and the immune system: (h) the structure and general functions of antibodies lesson, made from checked teaching notes for this specification point.

    Have a go first

    Which class of biological molecule are antibodies made from?

    Listen

    Antibodies are globular glycoproteins of the immunoglobulin family, secreted by plasma cells (differentiated B lymphocytes) in response to a specific antigen. Each antibody is a Y-shaped molecule of four polypeptide chains: two identical heavy chains and two identical light chains, held by disulfide bridges. The variable regions at the tips of the two arms form the antigen-binding sites, giving each antibody two identical binding sites and a shape complementary to one specific antigen. The constant regions are the same within a class and allow recognition by phagocytes and complement. General functions: binding to antigen to neutralise pathogens or toxins, marking them for destruction, and forming antigen–antibody complexes that can be destroyed by phagocytosis. Binding is specific and reversible. A strong answer earns marks for these points. Antibodies are proteins (globular glycoproteins/immunoglobulins) secreted by plasma cells derived from B lymphocytes. Each antibody has four polypeptide chains: two heavy and two light chains, joined by disulfide bridges. The Y-shaped molecule has two variable regions forming two identical antigen-binding sites. The binding site shape is complementary to a specific antigen, so binding is specific. Exam tip: Learn the four-chain Y structure with two heavy and two light chains and label the variable and constant regions.

    See it

    A top-down flowchart. The top node reads 'Antibody: globular glycoprotein (immunoglobulin)' and points to 'Four polypeptide chains'. This splits into two nodes, 'Two heavy chains' and 'Two light chains', both of which lead to 'Held by disulfide bridges', then to 'Y-shaped molecule'. The Y-shaped molecule node splits into 'Variable regions at tips of arms' and 'Constant regions'. The variable regions node leads to 'Two identical antigen-binding sites, complementary to a specific antigen'. The constant regions node leads to 'Same within a class; allow recognition by phagocytes and complement'. Both of these final nodes lead to a single node reading 'Functions: neutralise pathogens or toxins; mark antigens for destruction; form antigen-antibody complexes removed by phagocytosis'.
    Shows how the four-chain Y-shaped antibody structure, with its variable and constant regions, relates to specific antigen binding and to the general functions of antibodies.

    Key words

    Say what each word means before you turn the card.

    Antibody structure

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    Specificity of antigen binding

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    Role of plasma cells

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    Antibody function in immune defence

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    See every definition
    Antibody structure
    A Y-shaped molecule of four polypeptide chains: two identical heavy chains and two identical light chains, held by disulfide bridges.
    Specificity of antigen binding
    The variable regions at the tips of the two arms form the antigen-binding sites, giving a shape complementary to one specific antigen.
    Role of plasma cells
    Differentiated B lymphocytes that secrete antibodies in response to a specific antigen.
    Antibody function in immune defence
    Binding to antigen to neutralise pathogens or toxins, marking them for destruction, and forming antigen–antibody complexes destroyed by phagocytosis.

    Label the diagram

    Some boxes have lost their names. Pick the right name for each number.

    The diagram again, with 3 boxes numbered instead of named. A top-down flowchart. The top node reads 'Antibody: globular glycoprotein (immunoglobulin)' and points to 'Four polypeptide chains'. This splits into two nodes, 'Two heavy chains' and 'Two light chains', both of which lead to 'Held by disulfide bridges', then to 'Y-shaped molecule'. The Y-shaped molecule node splits into 'Variable regions at tips of arms' and 'Constant regions'. The variable regions node leads to 'Two identical antigen-binding sites, complementary to a specific antigen'. The constant regions node leads to 'Same within a class; allow recognition by phagocytes and complement'. Both of these final nodes lead to a single node reading 'Functions: neutralise pathogens or toxins; mark antigens for destruction; form antigen-antibody complexes removed by phagocytosis'.
    • 1Box 1

    • 2Box 2

    • 3Box 3

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