Родни Портер

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Scientific Accomplishments Rodney was awarded the 1972 Nobel Prize in Physiology or Medicine jointly with Gerald M. Edelman for their related but independent work that established the chemical structure of antibodies. Together, Porter and Edelman are recognized as having provided much of the foundation for the developing field of molecular immunology. Their groundbreaking work of the late 1950s and early 1960s ushered in a new era of research on antibodies, which previously had been only vaguely understood.

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Porter's most fundamental contribution was his hypothesis that antibodies had a Y-shaped structure. Having completed his doctorate Porter joined the scientific staff of the National Institute for Medical Research at Mill Hill, then directed by Sir Charles Harrington. Here he collaborated with A.J.P.Martin (also to become a Nobel Laureate). Martin was also concerned with structural analysis and this may have confirmed Porter's conviction that he was a protein chemist working in the field of immunology. It was during his time at Mill Hill that he initiated the work that was to uncover the basic structure of antibody molecules. Their protein nature had already been established but their structure was puzzling. In Cambridge Porter had worked with Sanger on the determination of the N-terminal amino acids in protein sequences. On the basis of analyses on immunoglobulins ( IgGs )

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Porter first believed antibodies had a single peptide chain and that their different specificities might be generated by differential folding., using the enzyme papain , he succeeded in splitting rabbit immunoglobulin G ( IgG ) into three parts: a large component that had no antigen-binding capability (the base of the Y) and two smaller fragments with active sites that bound to the antigen (the Y's arms). He demonstrated that the large fragment, or fragment crystallizable , was the same across all IgG molecules, but the two smaller fragments, which he called fragment antigen-binding ( Fab ), varied among antibodies.

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Based on his own research and that of Edelman, Porter correctly surmised that each Fab fragment consisted of two polypeptide chains and that each antibody was composed of four polypeptide chains: two long, heavy chains and two short, light chains. The heavy chains lie parallel for a distance, forming the Y's base. On the other end, they spread apart, forming two arms, each with a light chain attached parallel to it, with the highly variable, antigen-binding site, comprised of the N-terminal regions of both the heavy and light chains, at the ends of the arms.

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Porter's later research focused on both the role of antibodies as cell surface receptors and the complement system. His laboratory investigated the structure and genetics of members of the complex protein cascades constituting the complement activation pathways and the involvement of antibodies in complement activation.

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Porter was "one of the most outstanding biochemists in this country and in the world," said George Radda , a colleague of Porter's at Oxford .

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"I think his work probably changed the nature of the way we can think of combating diseases in terms of immunization and vaccination."The understanding of antibody structure and its implications for antibody function led to extensive exploration of the potential uses for antibodies in the development of therapeutics and vaccines.

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Dolores Ramos-Bello and Luis Llorente of the National Institute of Medical Sciences and Nutrition Salvador Zubirán in Mexico City concurred: "When Rodney R. Porter decided to perform molecular surgery on the antibody, he was unaware that he was lighting the match that would start a fireworks show in immunology."

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Biography Porter was born in Newton-le-Willows, near Liverpool on October 8, 1917. Rodney Porter was the perfect example of a scientist in the right place at the right time. The son of a railway clerk, he once told an interviewer that he did not "know why I became interested in [science]. It didn't run in my family." Nevertheless, he was fascinated with science, especially chemistry, at an early age and, in 1939, earned his B.S. in biochemistry at Liverpool University.

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During the Second World War, he served in the Royal Artillery, the Royal Engineers, and the Royal Army Service Corps, taking part in the North African, Sicilian, and Italian campaigns. Discharged in 1946, he began graduate study in biochemistry at Cambridge University, earning his Ph.D. in 1948 under Frederick Sanger. Inspired by Karl Landsteiner's (president 1927–28) The Specificity of Serological Reactions (1936) . Karl Landsteiner's (president 1927–28)

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Porter began studying antibodies and wrote his dissertation on methods of seeking antibodies active sites. As Sanger had before him, Porter soon gained a reputation for extreme persistence in pursuing a line of research that he believed promising, even if it appeared to be out of general favor.

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After completing his doctorate, Porter spent another year at Cambridge as a postdoctoral fellow. While at the National Institute for Medical Research at Mill Hill, London, from 1949 until 1960, he carried out the series of experiments that led to the successful fracturing of antibodies. In 1960, he became professor of immunology at St.

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Mary's Hospital Medical School, where he remained until accepting an appointment as Whitley Professor of Biochemistry and chair of the Department of Biochemistry at Oxford University in 1967. He had planned to retire from this position in 1985 to continue his research as director of the Immunochemistry Unit of the Medical Research Council. On September 6, 1985, only weeks before his retirement date, he died in an automobile accident at the age of 67.

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Awards and Honors Porter was a fellow of the Royal Society (1964) and a foreign member of the American Academy of Arts and Sciences (1968) and the National Academy of Sciences (1972). Porter was named a Companion of Honor by Queen Elizabeth II in 1985. In addition to the Nobel Prize, Porter received the Gairdner Foundation Award (1966), the Ciba Medal (1967), and the Karl Landsteiner Memorial Award (1968).