Rodney R. Porter

Most Popular

Rodney Robert Porter was an English scientist who shared the Nobel Prize in Physiology or Medicine in 1972 with Gerald M. Edelman. The award was given to the couple for their findings about the chemical structure of antibodies. Porter has been attracted by science since he was a child. He went on to study biochemistry at the University of Liverpool and subsequently fought in the British Army during World War II. He enrolled at the University of Cambridge to pursue his doctorate shortly after being dismissed from the army. His dissertation focused on methods for locating the active regions of antibodies, a topic on which he had spent nearly his whole life. He discovered that an antibody, also known as immunoglobulin, is made up of four chains of amino acids and is shaped like a Y. He also discovered that they were made up of three domains, two of which could bind the antigen and the third of which connected the two heavy chains. Later, he constructed an antibody model. Gerald Edelman, who was working on the same topic at the time, had gone ahead of him. Surprisingly, they were never competitors and instead took inspiration from one other’s work. Together they developed the field of molecular immunology, which had a far reaching influence on medical science.

Childhood and Adolescence

Rodney Robert Porter was born in Newton-le-Willows, a market town halfway between Liverpool and Manchester, on October 8, 1917. Joseph L. Porter, his father, worked as a railway clerk. Isobel Reese Porter was his mother’s name. His parents raised him as their only child.

Rodney Porter has always been captivated by science, particularly chemistry, since he was a child. He attended Ashton-in-Makerfield Grammar School in Ashton-in-Makerfield, Greater Manchester, for his secondary education, graduating in 1935.

He went on to the University of Liverpool, where he received his B.S. in biochemistry in 1939. When the Second World War broke out, he enlisted in the Royal Artillery, Royal Engineers, and Royal Army Service Corps, serving in the North African, Sicilian, and Italian campaigns, respectively.

Porter enrolled as a graduate student at the University of Cambridge after being dismissed from the army in 1946. He decided to study antibodies after reading Karl Landsteiner’s ‘The Specificity of Serological Reactions’ (1936).
Porter authored his dissertation on ways of identifying antibodies’ active sites while working under Frederick Sanger, a two-time Nobel Laureate, and received his PhD in 1948. ‘The free amino groups of proteins,’ was the title of his doctoral dissertation.

Career of Rodney R. Porter

Porter worked as a postdoctoral scholar at the University of Cambridge for a year after getting his PhD in 1948.
He began working as a scientific staff member at the National Institute for Medical Research in Mill Hill in 1949 and remained there until 1960. Porter continued his antibody study, which he had begun as a doctorate student.

Until then, all that was known about antibodies, also known as immunoglobulin, was that they were groups of proteins found in our blood that played a crucial part in fighting our bodies against infections and diseases. Scientists knew very little about their nature and mechanism of action before that.

Porter started by looking into antibodies’ molecular structure. He then decided to divide these antibodies in order to find out which sections were responsible for specific reactivity. He was particularly interested in chromatographic fractionation procedures.

Porter and his team used a protein-splitting enzyme called papain to treat the antibodies under controlled conditions in 1958-1959. The treatment split the antibody into three distinct functional fragments. He then began to research each component.

Porter left the National Institute for Medical Research in 1960 to become Pfizer Professor of Immunology at St. Mary’s Hospital Medical School, London University. He kept working on the antibody’s divided portions here.

As a result, he discovered that two of an antibody’s three segments were almost identical, while the third was functionally distinct. He also discovered that these identical parts could bind the antigen, whereas the third segment had various biological properties yet was unable to do so.

He proposed the peptide chain structure of antibodies in 1962. He established that these antibodies were constituted of four chains of amino acids; two of which were identical light chains while the other two were identical heavy chains. He then proceeded to develop an antibody model.

Porter moved again in 1967, this time to the University of Oxford as Whitley Professor of Biochemistry. He was also made a Fellow of Trinity College, Oxford, and chaired the Department of Biochemistry. He continued to work on antibodies here as well.

Porter was finally able to develop a comprehensive model of an antibody in 1969, consisting of 1300 amino acids. However, an American scientist named Gerald Edelman, who was working on the same subject at the time, was marginally ahead of him in developing this model. Nonetheless, Porter’s contribution to the research of immunoglobulin was lauded, and he was awarded the Nobel Prize.

Porter then teamed together with other scientists like Kenneth BM Reid, Robert Sim, and Duncan Campbell to learn more about the Complement Proteins involved in infection defense. Until his death in 1985, he continued to work at the University of Oxford.

Major Projects of Rodney R. Porter

Porter was the first to notice the Y-shaped structure of antibodies. He was also the first to employ enzyme papain to break it off at the point of branching and split it up into three segments. His key contribution was identifying the immunoglobulin’s antibody-binding (Fab) and antibody tail (Fc) regions.

Despite the fact that Gerald Edelman was the first to create an identical duplicate of an antibody, his work was no less important. In reality, the two scientists frequently drew on one other’s work while working on the subject. Although they worked independently, they were able to deduce the structure of the antibody together.

Achievements & Awards

Porter was honored with the Gairdner Foundation International Award in 1966 for his remarkable contribution to medical science.

Rodney R. Porter and Gerald Edelman won the Nobel Prize in Physiology or Medicine in 1972 for “discoveries relating the chemical structure of antibodies.”
“In honor of his profound investigations on the structure of immunoglobulins,” he was awarded the Royal Medal in 1973.

In 1983, he was awarded the Copley Medal for “elucidating the structure of immunoglobulins and the mechanisms involved in the activation of the complement system of proteins.”
On June 15, 1985, Queen Elizabeth II bestowed the Order of the Companions of Honour upon him.

Personal History and Legacy

Rodney R. Porter and Julia Frances New Porter married in 1948. The marriage had five children: Nigel and Tim Porter, two sons, and Susan, Ruth, and Helen Porter, three daughters.

Porter died in a car accident near Winchester, Hampshire, on September 6, 1985. He was just 67 years old at the time, yet his wife and five children survived him.

Estimated Net Worth

The estimated net worth of Rodney R. Porter is unknown.