Professor Rodney Porter
Born 8th October, 1917 (Newton le Willows, Lancashire, United Kingdom) - Died 6th September, 1985 (Winchester, United Kingdom)
Described by many colleagues as the father of modern immuno-chemistry, Rodney Porter was one of the most outstanding biochemists of his generation. He devoted his whole scientific life to the study of the immune system. In 1972 he was awarded the Nobel Prize for Physiology or Medicine, jointly with Gerald M. Edelman. Their methods showed the antibody molecule to be made up of two long, heavy protein chains and two identical shorter, lighter chains which combine to form a Y-shaped structure. This provided a key to understanding the function of one of the key components of the immune system, which is central to the development of effective diagnostics and therapeutics.
Rodney (Rod to his friends) was the younger of two sons born to his parents. As was common for the period Porter’s father, Joseph, left school at the age of 12 and went on to become Chief Clerk at the Earlestown Railway Carriage and Wagon Works, near Newton le Willows, a market town near Liverpool. An avid reader, Joseph was an early member of the Workers’ Educational Association, a voluntary organisation founded in 1903 to provide adult education, and was secretary for one of the Association’s local branches. A Wesleyan Methodist, with lots of humorous anecdotes to tell, Joseph was often called upon to be a speaker for local functions and Sunday school. Porter’s mother, May, was a highly intelligent woman who valued education and started her working life as a school teacher. Unable to continue her career after marriage, May taught both her sons and grandchildren to read before they started school. Coming from a farming background she also had a passion for the countryside which she passed on to Porter who retained a love of the outdoors for his whole life (Perry).
A keen sportsman, Porter played goalkeeper as an adolescent for the Wesleyans in the local Football League, dressed in the required cloth cap and green jersey. Once at university he continued to be a goalkeeper, playing for the Wesleyans in the Sunday School Association Football League. He also loved mountaineering and rock climbing, spending many weekends away on climbing trips. A tall man who walked with long loping strides, Porter often left others breathlessly trying to keep up. Described by his friends and colleagues as a good companion with a strong sense of fun, Porter was known for his forthright and heart-warming character (Perry).
Porter married Julia New in 1948. The two of them met while Porter was studying as a doctoral student in the Biochemistry Department at Cambridge University and Julia was working as a research assistant in the Physiology Department. They first connected when Julia was sent over to learn chromatography at the Biochemistry Department. Porter was assigned by his doctoral supervisor, Fred Sanger, to show her the technique. He was the most obvious one to teach her as he was using it for his research. Their engagement was announced not long after a holiday to Switzerland where Julia acquired Porter’s enthusiasm for the outdoors. They had five children together, the last two being twins. All the children were born in London while Porter was working at the National Institute for Medical Research in Mill Hill (Perry).
Porter always made sure to maintain a good balance between his work and time with his family. When Porter was appointed a professor at Oxford University, in 1967, he and Julia bought a farmhouse, Downhill Farm, with 13 acres which enabled them both to enjoy the countryside and become expert gardeners and bee-keepers. Porter also took up fishing but rarely caught anything. Over the years, many colleagues and visitors from abroad were invited to join the family at Downhill Farm and were made very welcome, often being enrolled into apple harvesting, chopping wood, dry-wall construction or going for long walks (Cohen).
Like his father, Porter read very widely and loved poetry. He also enjoyed opera and visits to the theatre, particularly to see Irish playwrights like Sean O’Casey. He followed current affairs closely and had a strong sense of injustice, supporting many causes to help people who were suffering (Perry).
Tragically Porter died three weeks before he was due to take official retirement. He was killed in a road accident while driving to go on vacation in France. Fortunately Julia was not seriously injured.
Porter attended the local primary school and then went to Ashton-in-Makerfield Grammar School. While not a particularly remarkable pupil, Porter managed to pass the School and Higher School Certificate Examinations in 1935. This provided him with the qualification to go to Liverpool University to study chemistry. But he was required to do a Preliminary Year to get his skills up to scratch before he could start his honour's degree in 1936. A late developer, Porter only began to show his true academic ability after starting his degree. He was awarded a first class Honours BSC in Biochemistry in 1939 (Perry).
Always keen to learn something new, Porter developed an interest in the application of chemistry to biology in his second year at university. Biochemistry was still a very new subject at the time. Fortunately for Porter, however, Liverpool was one of the few universities that had a Biochemistry Department, so he was able to transfer to it for his final year of study. It was here that he really began to flourish and show his promise as a researcher.
As well as graduating top of his year, Porter was awarded the Johnson Colonial Fellowship which enabled him to start a doctorate at Liverpool University under the supervision of A.P Platt focusing on lipid metabolism. His doctoral research was soon interrupted, however, by the outbreak of World War II. For a while life in the laboratory was able to carry on as normal, but by the summer of 1940 conditions had deteriorated so much that it was clear he could not continue his doctorate with Platt.
It was only after the war that Porter managed to get his doctorate. This he completed at Cambridge University in 1948 under the supervision of Fred Sanger. His dissertation was on haemoglobins, a protein carried by red blood cells which helps to pick up oxygen in the lung and distribute it to peripheral tissues. His doctoral studies were initially supported by an ex-Serviceman’s grant supplemented by his wartime savings (Perry).
Throughout his student days, Porter could be found in the thick of action, taking part in horseplay and water fights with his peers. However, whenever he came under stress he developed a stutter which made speaking in public difficult and made him slightly unsure of himself. He eventually overcame the problem through determination and application (Perry).
Like many people with a scientific degree, Porter could have entered a safe reserved occupation during the war. But instead he chose to serve in the Royal Artillery. Not called up immediately, because of the lack of training facilities, Porter initially carried on working with Platt while participating in the university’s Officer Training Corps. The Corps was made up of students who spent their lunchtimes and evenings marching up and down outside the biochemistry building to get fit and did labouring work for a farm near Chipping Campden in the Cotswolds.
In the autumn of 1940 Porter joined the survey section of the Artillery as a private. Not enjoying the duties, which involved surveying gun positions, and having little prospects of advancement, in January 1942 Porter transferred to the Officer Cadet Training Unit and six months later joined the Royal Engineers. In October 1942 he took part in the First Army landing in North Africa and then as the campaign progressed moved on to Sicily and then Italy. While in Italy he met up with his brother, who was also fighting there, who told him of a position as a War Department analyst. He secured the post on the back of his scientific qualifications. By the end of the war Porter had risen to the rank of Major (Perry).
Discharged from the army, in December 1945, Porter was eager to get back to doing a doctorate. Unable to return to Platt, because he had died, Porter was taken on by Frederick Sanger, an expert in protein chemistry in the Biochemistry department at Cambridge University. Porter joined Sanger as his first doctoral student in 1947. At the time Sanger was in the process of developing a sequencing method to unravel the amino acid composition of insulin, a small protein secreted by the pancreas that helps to regulate sugar levels in the blood. This he completed in 1955, paving the way for him to win the Nobel Prize in 1958. Working together in a relatively small basement laboratory in the Department of Biochemistry, Sanger and Porter were very well suited as they shared a tenacity of purpose and ability to persist with a challenge when most others thought the task impossible (Perry).
Porter’s time with Sanger was invaluable for equipping him with the skills to do protein sequencing which was enormously beneficial to his future career in biochemistry. In particular it set him up well to contemplate unravelling the chemical structure of antibodies which in the 1950s remained a mystery. Sanger was also very encouraging of his work in this area, which was especially regarded by most researchers as too daunting to undertake. Porter first became inspired to work on the issue after reading Karl Landsteiner's book The Specificity of Serological Reactions (1936, 2nd edition 1946). What particularly fascinated Porter was how the body could produce so many different kinds of antibodies that could bind so specifically to an infinite range of targets (Perry).
Another person who proved important to Porter in Cambridge was Albert Chibnall, the head of the Biochemistry Department. He had the foresight to realise that Porter would struggle to get a lectureship once he finished his doctorate because of his speech impediment. For this reason Chibnall approached Sir Charles Harington, the director of the National Institute for Medical Research, in Mill Hill, to offer Porter a research position. Harington was familiar with Porter’s work because he had been his external PhD examiner and quickly agreed to take him on once new laboratory space had been built. Unable to be accommodated immediately in Mill Hill, Chibnall arranged for Porter to stay on in Cambridge with a grant of £650 from the Medical Research Council to work on the structure of antibodies and diphtheria toxin (Perry).
Porter moved to the Institute in 1949, where he continued to work on antibodies. In October 1955, Betty Press, a protein chemist, joined Porter’s small research group, now consisting of two technicians. A modest and understated person, Press played a significant role in helping Porter to break down the antibody molecule into fragments and chains. She was co-author of many publications with Porter including a major one on the determination of the four-chain structure of the antibody molecule (Fleischman, Porter, Press), for which Porter was awarded the Nobel Prize in 1972. Press carried on working alongside Porter for the next twenty five years, moving with him to different institutions (Hogg, Steiner).
In 1960 Porter was appointed the Pfizer Professor of Immunology in the Wright Fleming Institute of Microbiology at St Mary’s Hospital Medical School. It was the first Chair of Immunology in the country. Getting the position was not a foregone conclusion. All three external advisors for the post, professors of bacteriology in medical schools in London, advised against his appointment because he did not have any medical qualifications. The new position at St Mary’s not only provided Porter with five times more laboratory space than he had in Mill Hill but two established university posts. One post went to Press and the other to Sydney Cohen who, being medically qualified, was assigned to teach medical students for the department (Perry).
Porter remained at St Mary’s for seven years. These years proved highly productive and it was during this time that Porter and his team managed to break down the antibody molecule into fragments which laid the basis for understanding the antibody structure. He soon became a well-respected, international figure in his field. Researchers came from all over the world to work with his team and he was invited to speak at international meetings about immunology. Porter enjoyed working with groups of colleagues with whom he could discuss ideas and was a great supporter of international cooperation. He was happy to provide advice, but never took credit for work done by other people, often encouraging them to publish independently. Overall he is thought to have worked alongside more than 120 different people over his career, many of whom went on to contribute substantial research to the field.
As one of the most distinguished British biochemists in his age group, Porter was elected to become a member of the Royal Society Society in 1964, at the age of 46. Two years later he was presented with the prestigious Award of Merit of the Gairdner Foundation and in 1967 the Ciba Medal of the Biochemistry Society. He was also awarded the Karl Landsteiner Award of the American Association of Blood Banks in 1968. By this point he had also been chosen by Oxford University to succeed Sir Hans Krebs on his retirement from the Whitley Chair of Biochemistry.
Following his appointment to Oxford, in 1967, Porter quickly secured funding from the Medical Research Council to set up an Immunochemistry Unit under his direction. This was important because it freed him up from the necessity of having to make regular applications for grants to support his research. Nonetheless, his new role required him to take on administrative responsibilities for the first time. Expected to chair departmental staff meetings Porter quickly showed his abilities in this area. He took a great interest in the careers of his students and colleagues and, although teaching was not his favourite occupation, he gave lectures to undergraduates. Immunology had not previously been part of the Oxford University curriculum. For the first time in Porter’s career, research was not his full time occupation, but he kept in close contact with the work, and spent at least part of most days in the laboratory.
As a senior staff member of the university, Porter also served on many different committees and was a delegate for Oxford University Press (1972-82) as well as a curator for the Botanical Gardens. This he did alongside acting as an adviser to many organisations outside the university, including for the Medical Research Council, Biological Sciences Board, and the Royal Society. He also sat on a number of committees concerned with the allocation of research funds and fellowships, including the Imperial Cancer Research Fund Committee, the Beit Memorial Fellowships Committee, the 1851 Science Scholarships Committee and the Advisory Board of the Basle Institute of Immunology. Porter also served on the editorial boards of the Biochemical, Archives of Biochemistry, Immunochemistry and the European and Scandinavian Journal of Immunology, and established a rapid publication journal for the Biochemistry Society: Bioscience Reports. He also used his influence to raise funds for a number of worthwhile causes, such as the construction of the Rex Richards Building for the MRC. Immunochemistry Unit, the Enzyme NMR. Group and Biophysics.
In 1981 Porter played a critical role in helping to raise funds to buy Edward Jenner’s House to turn it into a museum and conference centre. Porter saw Jenner as an extremely important figure in immunology because of his discovery of vaccination. One of the exhibits in the museum includes Porter’s laboratory notebook describing the splitting of immunoglobulin molecules.
Porter’s first achievement was made at Mill Hill together with Archer J P Martin, a pioneer of column chromatography. In 1951 they demonstrated for the first time that it was possible to separate ribonuclease into two homogeneous forms using column chromatography (Martin, Porter ). Ribonuclease is a small protein that helps to break down RNA. Porter and Martin prepared the ribonuclease from ox pancreas. It was one of the first proteins to be fractionated with partition chromatography. Martin was jointly awarded the Nobel Prize in Chemistry a year later for his work on chromatography.
Following the work on ribonuclease, Porter spent a number of years trying to improve the chromatography method for use with other proteins. This led him to develop a single chromatographic step which provided a means to isolate insulin from tissue extracts. Considered to have potential for commercial application, a provisional patent was taken out on Porter’s technique.
But the real interest Porter had in chromatography was to use it to break down the antibody molecule into clean and small enough fragments that would make it possible to carry out amino acid analysis. This was important because intact antibodies were too large for existing methods of amino acid analysis. By 1955 Porter had managed to separate antibodies into several distinct fractions using a technique of partition chromatography he had devised, but he concluded that that his method would never allow for complete fractionation.
In order to resolve the problem Porter decided to revisit the use of papain, which he had attempted to use during his doctoral research in Cambridge to fractionate immunoglobulin from rabbits. At the time he had only had access to crude papain so his experiments had proven unsuccessful. By 1957 a purer form of papain had become available so in 1958 Porter decided to repeat his earlier experiment. To his delight the papain enzyme cleaved the antibody into three pieces of similar size which he was able to separate using newly available ion exchange chromatography. Two of the fragments had identical structures and appeared to comprise the region of the antibody that bound to antigens, receptors found on the outside of any substance foreign to the body. For this reason they were called the antigen-binding fragment (Fab). The third fragment had a very different chemical structure. Initially Porter thought it was a crystal of cystine and an artefact of his method so he kept pouring it down the sink. It soon became clear that in fact it was the tail region of an antibody, now called the fragment crystallisable region (FC), which helps activate the immune system.
Porter published his findings in 1959. In the same year Gerald Edelman, an American immunologist working at the Rockefeller University in New York discovered that it was possible to break down human immunoglobulin using mercaptoethanol and concluded that there were several polypeptide chains in the molecule. Porter’s team quickly picked up on Edelman’s result and produced two fractions: the A fragment contained the heavy chains and the B fragment contained the lighter chains. Gel filtration suggested that there could be two A and two B chains. This result showed the importance of strong international contacts because the antibodies used in the UK research were brought by Fleischman from the USA. In March 1962 Porter proposed a four-chain structure for immunoglobulin at a meeting in New York, although there was still some uncertainty over it. Further work confirmed the four-chain structure, but did not explain the wide range of specificities, and it was not clear whether both chains were involved in the antigen/antibody process. However, this was the work that earned the two men a Nobel prize.
After establishing the detailed structure of immunoglobulin molecules, Porter turned his attention to the role of antibodies as cell surface receptors. He also began work on the complement system. As had been the case with antibodies in 1948, the complement system was still unexplored territory for biochemists in the 1970s. What interested him was how antibodies helped to prompt a cascading series of protein reactions to mobilise different cells in the immune system to destroy foreign substances.
When it became clear that such work needed him to move into immunogenetics, including gene cloning and sequencing, Porter, then in his mid-sixties, decided to take time away from his desk to learn these new techniques. Over the following few years leading up to his compulsory retirement, Porter and his team undertook a great deal more valuable work building on the new knowledge he had gained. In particular, they proposed the theory that susceptibility to a particular autoimmune disease was due to polymorphism in the complement system. Porter planned to continue working in this area of research after his official retirement, but sadly this was not to be because of his untimely death. However, he left behind him an important programme of research for his research team to continue which focused on genes in the major histocompatibility complex.
Alongside winning the Nobel Prize in 1972, Porter’s achievements were recognised by the award of many different honours appropriate to a biochemist of his distinction. Shortly before he died, in 1985 he was made the Companion of Honour by Queen Elizabeth II. It is thought that he refused a knighthood because he did not want to be called ‘Sir Rodney’. This was reflective of his abhorrence for any pomposity. Throughout his life he valued the qualities of honesty, simplicity, firmness and understanding. Always down-to earth, he never talked about his achievements and awards (Cohen;Perry).
This a documentary produced by Swedish TV about the scientists Rodney Porter and Gerald Edelman around the time of their Nobel Prize win. Credit: Swedish Broadcasting Corporation, 1972. For those who do not have time to watch the complete film the following segments are interesting: 5:30-7:54 explains the chain structure of antibodies, their active sites and how they function with foreign invaders; 8:55-10:00 talks about the enigma of how antibodies are formed; and 11:31-18:23 which gives a glimpse into Porter's home life and his thoughts about antibodies and the complement system.
This profile was written by Helen Howard and Lara Marks, 1 July 2020. We are grateful to Nigel Porter for his help in compiling this profile and generous sharing of the family photographs.
Fleischman, JB, Porter, RR, Press, EM (1963), ‘The arrangements of the peptide chains of y-Globulin’, Biochemistry Journal, 88, 220-28. Back
Johnstone, AP, Kerr, MA, Turner, MW, ‘Obituary: Rodney Robert Porter ( 1917-1985)’, Journal of Immunological Methods, 85 (1985), pp. 1-4. Back
Martin, AJP, Porter RR (July 1951), ‘The chromatographic fractionation of ribonuclease’, The Biochemical Journal, 49/2, 215-8. Back
Rodney Porter: timeline of key events
|8 Oct 1917||Rodney R Porter was born in Newton-le-Willows, United Kingdom||Porter||Oxford University|
|July 1951||Ribonulcease separated into two homogenous forms using column chromatography||Porter, Martin||National Institute for Medical Research|
|1962||Antibodies discovered to have structure like a 'Y'||Porter, Edelman||National Institute for Medical Research, Rockefeller University|
|1 Jan 1972||Nobel Prize awarded to Gerald Edelman and Rodney Porter for discovery of antibody chain-like structure||Edelman, Porter|
|7 Sep 1985||Rodney R Porter died||Porter||Oxford University|
8 Oct 1917
Rodney R Porter was born in Newton-le-Willows, United Kingdom
Ribonulcease separated into two homogenous forms using column chromatography
Antibodies discovered to have structure like a 'Y'
1 Jan 1972
Nobel Prize awarded to Gerald Edelman and Rodney Porter for discovery of antibody chain-like structure
7 Sep 1985
Rodney R Porter died