b.8 October 1917 d.6 September 1985
CH(1985) BSC Liverp(1939) PhD Cantab(1949) FRS(1964) Hon FRCP(1974) Nobel Laureate Medicine(1972)
Rodney Porter was born at Newton-le-Willows, Lancashire, the son of Joseph and Isabel Porter. He died in a road accident while driving from Oxford to Plymouth just three weeks before he was due to retire as Whitley professor of biochemistry at Oxford. He made outstanding contributions to immunochemistry and was largely responsible for elucidating the chemical structure of antibodies; for this work he was awarded, jointly with G M Edelman, the Nobel Prize in medicine in 1972. He received many other honours, including the Royal Medal (1972) and Copley Medal (1983) of the Royal Society, foreign membership of the American Academy of Sciences (1972) and Companion of Honour (1985).
Rodney was educated at Ashton-in-Makerfield Grammar School and Liverpool University, where he took his BSc honours in 1939. For the next six years he served in the Army, mainly in the Mediterranean theatre with the Royal Engineers, and was discharged in December 1945 with the rank of major, Royal Army Service Corps. He then went to Cambridge where he worked with Fred Sanger, then engaged in elucidating the structure of insulin for which he was awarded the Nobel Prize some 10 years later. It was at Cambridge that Porter developed his lifelong fascination with protein chemistry, and he always thought of himself as a protein chemist devoted to immunology. His particular interest in immunochemistry was stimulated by reading Landsteiner's classic monograph The Specificity of serological reactions, revised edition, New York, Dover Publications, 1962, a small book that inspired a generation of immunologists. Since most antibodies have identical overall molecular properties and antigenicity, their endless diversity of combining specificity provided a striking paradox. As Porter remarked in the Nobel lecture [Science 180:713-6,1973] ‘This combination of an apparently infnite range of antibody combining specificity associated with what appeared to be a nearly homogeneous group of proteins astonished me and indeed still does.’
Porter left Cambridge in 1949 and joined the staff of the National Institute for Medical Research, working first with A J P Martin, soon to be awarded the 1952 Nobel Prize in chemistry for the development of chromatography. On the day of that award the young Dr Porter received an early morning phone call in the laboratory congratulating him on winning the Nobel Prize. The caller was a Swedish journalist somewhat confused by the fact that A J P Martin’s middle name happened to be Porter. Rodney later remarked that on receiving this encouraging news his mind had scanned with remarkable speed over the contents of his publication for that year and, excellent as it was, even he had to admit that a Nobel Prize appeared a little excessive! In later life Porter felt that he owed most to Sanger and Martin, and to Sir Charles Harington [Munk's Roll, Vol.VI, p.222], then director of the NIMR, who had given him invaluable encouragement.
It was at Mill Hill that Porter initiated the work that, within a decade, was to elucidate the basic structure of antibody molecules and provide the foundation for our current understanding of their molecular diversity and individual specificity. At that time the protein nature of antibodies had been confirmed, but their structure was totally mysterious and presented no obvious means of solution. Porter himself believed, on the basis of N-terminal amino acid analyses, that antibodies comprised a single polypeptide chain and that different specificities might be generated by differential folding of that chain. His inspirational approach to this problem was to fragment the molecule in the hope of obtaining smaller pieces which retained antibody activity and were more amenable to analysis. In 1958 he found that the enzyme papain cleaved rabbit IgG into three pieces of similar size; two were identical and retained the original combining specificity (Fab) while the remaining one crystallized (Fc). That protein quite incapable of crystallizing itself should yield a crystalline fragment was unthinkable, and Porter would later relate with wry pleasure how for several months he had disposed of Fc crystals down the sink believing that they were crystals of cystine derived from the cysteine used to activate papain. However, the finding of common and variable structures within a single protein molecule was the vital key to the solution of the antibody paradox, and the papain technique enabled the properties of antibodies, some common and some individually distinct, to be assigned to discrete portions of the molecule.
In 1960 Porter became the Pfizer professor of immunology at St Mary’s Hospital medical school, the first chair of immunology to be created in the United Kingdom. By this time, Gerald Edelman at the Rockefeller Institute had demonstrated that antibodies are multichain proteins. The problem of relating the papain pieces to the chains required isolation of the chains in soluble and undernatured form. This was accomplished by Porter soon after he moved to St Mary’s. Subsequent antigenic analysis of the heavy and light chains with antisera to the Fab and Fc fragments provided the data which clinched the four chain structure, first proposed by Porter in 1962. This stucture proved applicable to the antibodies of all vertebrate species. It led to the precise understanding of the chemical relationships which exist between different classes of antibodies as well as between those produced by normal and cancerous lymphoid tissues. The work also heralded a progressive understanding of immunological processes in molecular terms, which has given immunology its currently pervasive role in general biology and clinical medicine.
Porter succeeded Sir Hans Krebs [Munk’s Roll, Vol.VII, p.325] as Whitley professor of biochemistry at Oxford in 1967; inevitably he became heavily involved in teaching and administration and yet still found time actively to direct the MRC immunochemistry unit with outstanding success. The work of this unit focussed on the interaction of antibody-antigen complexes with the complement system. The molecular structure of Clq and of C4 were elucidated,the unexpected covalent binding of C4 to IgG was demonstrated, and as culmination his Oxford laboratory described the genes for C2, factor B and C4 and established their alignment in the MHC region of human chromosome 6. Porter had latterly become fascinated by the extensive polymorphism of C4 and the possible role of this in determining individual susceptibility to autoimmune disease. As he neared retirement from the Oxford chair, his research maintained momentum and the MRC, with customary wisdom, arranged that he should continue to direct the immunochemistry unit after he had vacated the chair of biochemistry.
Rodney Porter was an outstandingly successful scientist whose creative activity was unusually sustained. His early years were academically unremarkable and his first distinction, the fellowship of the Royal Society, did not come until the age of 47. His singular good fortune was, of course, to be a graduate student in Fred Sanger’s laboratory at the time when techniques for the detailed study of protein structure were being evolved for the first time. His own capacity to exploit that nascent experience derived from his innate tenacity and enviable capacity for direct and uncluttered thought. He was able to identify and focus upon the central issue of a problem and ignore irrelevant distractions. His laboratory might appear fairly chaotic to the uninitiated, but any promising experimental lead from an always pragmatic approach was consolidated and rapidly expanded by logical progression, based upon great technical expertise and painstakingly precise interpretation.
These same qualities of honesty, simplicity, firmness and understanding, illuminated Rod Porter’s personal life. He abhorred any hint of deviousness, pretence or pomposity. His many honours were received with robust enjoyment, but always tempered by a spicy irreverance which proclaimed his unshakeable identity. Over the years his endearing qualities served to transmute colleagues from near and far into lifelong friends. All were taken to Downhill Farm to enjoy the warmth of his wife Julia’s open-hearted hospitality, and very likely to be unceremoniously enrolled into apple harvesting, lumbering, bee-keeping, dry-wall construction or tramping many miles across the countryside. Rodney Porter was universally admired and respected as a scientist, but he will be most vividly remembered by countless friends and colleagues for his forthright and heart-warming character, which enriched innumerable lives.
[The Times, 9 Sept 1985; Roy.Soc News, July 1983,2,No 4,1; St. Mary’s Hosp. Gaz., 1960,66,212; Contemp.Scien.Arch.Centre,Prog.Report, 25,1985-1986]
(Volume VIII, page 388)
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