Rodney Robert Porter was a Nobel Prize winning English biochemist who won the 1972 Nobel Prize in Physiology or Medicine
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Rodney Robert Porter was a Nobel Prize winning English biochemist who won the 1972 Nobel Prize in Physiology or Medicine
Rodney R. Porter born at
In 1948, Rodney R. Porter married Julia Frances New Porter. The couple had five children; two sons, Nigel and Tim Porter, and three daughters, Susan, Ruth and Helen Porter.
On 6 September 1985, Porter died in a road accident near Winchester, Hampshire. He was only 67 years old then and was survived by his wife and five children.
Rodney Robert Porter was born on 8 October 1917, in Newton-le-Willows, a market town located midway between Liverpool and Manchester. His father, Joseph L. Porter, was a railway clerk. His mother’s name was Isobel Reese Porter. He was the only child of his parents.
From an early age, Rodney Porter was fascinated by science and was especially interested in chemistry. He had his secondary education at Ashton-in-Makerfield Grammar School, located in Ashton-in-Makerfiel, Greater Manchester, passing out from there in 1935.
Subsequently, he entered the University of Liverpool, earning his B.S degree in biochemistry in 1939. As the Second World War set in, he joined the British Army serving in the Royal Artillery, the Royal Engineers, and the Royal Army Service Corps respectively and took part in the North African, Sicilian, and Italian campaigns.
After being discharged in 1946, Porter enrolled at University of Cambridge as a graduate student. Inspired by Karl Landsteiner’s, ‘The Specificity of Serological Reactions’ (1936), he decided to study antibodies.
Working under Frederick Sanger, the two-time Nobel Prize winner, Porter wrote his dissertation on methods of seeking antibodies' active sites; finally receiving his PhD degree in 1948. His doctorate thesis was titled ‘The free amino groups of proteins’.
After receiving his PhD in 1948, Porter spent one more year at the University of Cambridge as a postdoctoral fellow.
In 1949, he joined the National Institute for Medical Research at Mill Hill as scientific staff and remained there till 1960. Here, Porter continued his research on antibodies, which he had started as a doctoral.
Until then, it was only known that these antibodies, also referred as immunoglobulin, were groups of proteins that played an important role in defending our body against infections and diseases and that they are found in our blood. Otherwise, scientists had very little knowledge about their nature and mechanism of action.
Porter began by studying the molecular structure of antibodies. Subsequently, he decided to split these antibodies in order to identify those parts, which were responsible for specific reactivity. He was especially interested on chromatographic methods of fractionation.
Sometime in 1958-1959, Porter and his team treated the antibodies with a protein-splitting enzyme called papain under controlled condition. The treatment divided the antibody into three functionally different segments. He then began to study each part.
Porter was first to recognize that antibodies had a Y-shaped structure. He was also the first to use enzyme papain to break it off at the point of branching and split it up into three segments. However, his main credit lay in identifying the antibody-binding (Fab) and the antibody tail (Fc) regions of the immunoglobulin
Although he was preceded by Gerald Edelman in creating an exact replica of an antibody, his contribution was no less significant. In fact, while working on the problem, the two scientists often drew upon each other’s work. It can be safely said that although they worked separately they together deduced the structure of the antibody.