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Description
This programme examines the structure of an antibody molecule and discusses some of the experiments which were done to determine it.
Metadata describing this Open University video programme
Module code and title: S322, Biochemistry and molecular biology
Item code: S322; 14
First transmission date: 15-09-1977
Published: 1977
Rights Statement:
Restrictions on use:
Duration: 00:24:00
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Producer: James Burge
Contributors: Gerald Edelman; Elvin Kabat; Rodney Porter; Martin Raff; Allen Edmundson
Publisher: BBC Open University
Keyword(s): Antibody; Antigen; Domain; Polypeptide chain
Footage description: Over film shots of a blood typing test being carried out and of T killer cells active in the blood stream, Martin Raff introduces the programme. Raff goes on to explain, briefly, the function of B lymphocytes. An animated diagram helps to illustrate his points. Gerald Edelman, in his office, explains how he and Prof. Porter discovered that the antibody molecule was composed of multiple polypeptide chains of two different kinds. Rodney Porter explains in more detail the methods used to split the antibody molecule and which showed that it was made up of two heavy and two light polypeptide chains. Porter writes on a blackboard as he talks. He goes on to explain the mechanism by which the chains are connected. Martin Raff sums up the programme so far. He places cards containing diagrams on a table as he talks. Raff explains a major problem which confronted biochemists who wished to determine the amino acid sequence of an antibody molecule - that of getting enough of a single type of antibody for assay. He goes on to explain how this problem was solved with the discovery that patients suffering from a particular cancer (multiple myeloma) had large amounts of a single type homogenous antibody in their serum. Gerald Edelman recalls how he used the multiple myeloma protein to work out the sequence of antibody light chain and later the heavy chain as well. Using strings of beads to simulate amino acid chain. Raff points out the distinct variable and constant regions of the antibody molecule for both light and heavy polypeptide chains. Elvin Kabat recalls how he and his colleagues predicted hypervariable regions within the variable regions of the antibody. He uses a graphics board and a histogram to help illustrate his points. Martin Raff discusses the discovery by Edelman in 1968 that both light and heavy chains of antibodies are made up of repeating regions and how this accounts for the folding of the chains to form compact, functional units. He uses several bead models to illustrate his points. Over shots of a protein crystal, Raff discusses the use of x-ray diffraction techniques to confirm the predictions of the immunochemists. Allen Edmundson explains what his studies of the NP Bentz-Jones protein crystal by x-ray diffraction, told about antigen binding sites and the shape of the antibody. He uses a low resolution molecular model of an antibody to illustrate his points. Raff sums up the programme with the aid of models.
Master spool number: 6HT/72638
Production number: 00525_1271
Videofinder number: 1021
Available to public: no