ImmunologyToday, vol. 6, No. 10, 1985
290
H](m Rodney Robert Porter FRS, CH
Professor Rodney Porter was killed in a car accident on 6 September, 1985. His death is a great sorrow to the scientific community and especially to those involved in immunological research. Although he was due to retire from the Whitley Chair of Biochemistry at Oxford on 1 October, 1985, he had planned to continue research in his capacity as Director of the MRC Immunochemistry Unit.
Rod Porter was born at Newton-leWillows in Lancashire on 8 October, 1917, and educated at Aston-in-Makerfield G r a m m a r School and at the University of Liverpool, from which he graduated with a BSc Honours degree in 1939. During the war he served with the Royal Engineers and was discharged in December 1945 with the rank of Major. He went to Cambridge to work with F. Sanger who was at that time engaged on his Nobel Prize winning studies involving the determination of the amino acid sequence of insulin. This start in research on protein chemistry with Sanger greatly influenced his career, and also while at Cambridge his interest in immunochemistry was stimulated by Landsteiner' s Specificity of SerologicalReactions (1945 edition) and Burnet & Fenner's 1941 publication The Production of Antibodies. With only a few breaks he continued to work in immunology for the rest of his career but he always maintained that he was best described as a protein chemist who worked in the field of immunology. After obtaining his PhD in 1949 he became a member of staff at
© 19S5, Elsevier Science Publishers B.V., Amsterdam
the National Institute for Medical Research, where he collaborated for several years with A. G. P. Martin (later to be awarded the Nobel Prize) learning the techniques of protein chromatography which formed an important basis of Rod's own work on antibody structure. His first papers on rabbit antibodies were published in 1950 but the bulk of his work on antibodies, while at Mill Hill, were published in the late 1950s and included the crucial 1958 Nature paper describing the limited proteolysis of antibody IgG by papain and the separation of the two Fab fragments, which retained specificity for antigen, and the third fragment, the Fc, which was crystallizable. In 1960 he became the Pfizer Professor of Immunology at St Mary's Hospital Medical School, London, the first Chair of Immunology to be created in the U K Following the finding by Gerald Edelman in 1959 that antibodies had a multichain structure, Rod and his colleagues were able to isolate the separate chains of IgG antibody in an undenatured form and relate them to the
0167-4919/85/$02.00
products of papain digestion. This allowed the proposal in 1962 of the now familiar four chain structure of IgG antibody. Amino acid sequence studies by Rod's group on the heavy chains from two h u m a n pathological IgGs and from pooled normal rabbit IgG, together with earlier studies by other laboratories on the light chains, provided evidence for the presence of variable and constant regions in the chains of IgG antibody. These structural studies helped solve the problem of how antibodies could recognize a vast range of different antigens yet react in a constant way with the molecules that triggered effector function subsequent to antibody binding. For his role in this work Rod was awarded the Nobel Prize for Physiology or Medicine jointly with Gerald Edelman in 1972. His move to Oxford University in 1967 as Whitley Professor of Biochemistry meant that he became heavily involved in teaching, administration and scientific committee work, yet he still managed to find time to successfully direct research in the M R C Immunochemistry Unit. His practical and direct approach to research was a feature throughout his career, as was his skill at stimulating and influencing the research of an international array of students, post-doctoral workers and visitors on sabbatical. All of these people felt a great respect and affection for Rod and valued the time spent in his laboratory. Much of his work at Oxford was involved with the mechanism by which antibody-antigen aggregates interacted with, and activated, the serum complement system and also with the detailed structural analysis of many of the complement components. In 1968-69 the Valentine and Green bivalent DNPhapten-anti D N P antibody system was used to show that well defined IgG complexes of tetramer size, or higher, efficiently bound and activated the C1 complex. Further work on IgQ, in the period 1971-73, allowed the characterization of Facb (fragment-antigen and complement binding) from plasmin digested IgG and helped define the CH2 domain as being the C 1 binding region. He then turned his attention directly to the complement system itself, and structural and functional studies on the subcomponents C 1q, C 1r and C ls occupied much of his interest during the period 1971-78. These studies included the proposal of a molecular model for the unusually shaped C l q molecule and a mechanism by which the C1 complex interacts with aggregated IgG to bring about activation of the proenzymes C l r and Cls. The activated C 1 complex enzymatically splits and activates C4, and an
Immunology Today, vol. 6, No. 10, 1985 interest in the functional role of C4 was central to Rod's personal research during the period 1978-85 which involved: sequencing the complex three chain protein; study of the covalent binding of activated C4 to the Fd region of IgG antibody; the demonstration that the different C4A and C4B types of C4 showed preferential binding to protein and polysaccharide, respectively; isolation of cDNA and genomic clones of C4 and studies on the genetics of C4. His group were also involved in work, at the protein and DNA levels, on C2 and factor B as well as C4, and the description and alignment of these Class III genes on chromosome 6 in the human M H C region in Nature (1984) was a highlight in his recent research. As more data on C4 accumulated, the possible role that allelic forms of C4A and C4B might play in determining an individual's susceptibility to autoimmune-type disease
291 became a major interest. It was remarkable that his research activity as he neared 'retirement' appeared to be increasing rather than decreasing. In the last few years he had been a prolific writer of articles and reviews and they all bore his characteristic clear, direct and brief style. He had a great ability to grasp quickly the essential points in a complex problem, be it scientific or administrative, and make a rapid assessment and decision. Throughout his career he received many prizes and honours, the most recent being the Companion of Honour awarded earlier this year, and he held many influential posts. However, one which gave him particular pleasure was appointment as a Curator of the Botanic Gardens at Oxford. His interests in gardening, bee keeping and other rural pursuits were carried out at his farmhouse where often an unsuspecting post-
doc would find himself engaged in some aspect of forestry or a wall-rebuilding programme. His relaxation away from Oxford was hill walking and he was very knowledgeable about the testing long walks and climbs throughout the U K and Continent. He and Julia had a knack of making the members of his Unit and visitors feel like one big family and the warmth of this feeling was well illustrated in July this year when many of his past co-workers gathered to form p a r t of a large audience which attended the Biochemical Society Symposium and Dinners held in his honour. It is a privilege to have been the friend and colleague of an outstanding scientist who had such a fine personality; he will be greatly missed. [~ KEN REID
M R C Immunochemistry Unit, Oxford, UK.
290
H](m Rodney Robert Porter FRS, CH
Professor Rodney Porter was killed in a car accident on 6 September, 1985. His death is a great sorrow to the scientific community and especially to those involved in immunological research. Although he was due to retire from the Whitley Chair of Biochemistry at Oxford on 1 October, 1985, he had planned to continue research in his capacity as Director of the MRC Immunochemistry Unit.
Rod Porter was born at Newton-leWillows in Lancashire on 8 October, 1917, and educated at Aston-in-Makerfield G r a m m a r School and at the University of Liverpool, from which he graduated with a BSc Honours degree in 1939. During the war he served with the Royal Engineers and was discharged in December 1945 with the rank of Major. He went to Cambridge to work with F. Sanger who was at that time engaged on his Nobel Prize winning studies involving the determination of the amino acid sequence of insulin. This start in research on protein chemistry with Sanger greatly influenced his career, and also while at Cambridge his interest in immunochemistry was stimulated by Landsteiner' s Specificity of SerologicalReactions (1945 edition) and Burnet & Fenner's 1941 publication The Production of Antibodies. With only a few breaks he continued to work in immunology for the rest of his career but he always maintained that he was best described as a protein chemist who worked in the field of immunology. After obtaining his PhD in 1949 he became a member of staff at
© 19S5, Elsevier Science Publishers B.V., Amsterdam
the National Institute for Medical Research, where he collaborated for several years with A. G. P. Martin (later to be awarded the Nobel Prize) learning the techniques of protein chromatography which formed an important basis of Rod's own work on antibody structure. His first papers on rabbit antibodies were published in 1950 but the bulk of his work on antibodies, while at Mill Hill, were published in the late 1950s and included the crucial 1958 Nature paper describing the limited proteolysis of antibody IgG by papain and the separation of the two Fab fragments, which retained specificity for antigen, and the third fragment, the Fc, which was crystallizable. In 1960 he became the Pfizer Professor of Immunology at St Mary's Hospital Medical School, London, the first Chair of Immunology to be created in the U K Following the finding by Gerald Edelman in 1959 that antibodies had a multichain structure, Rod and his colleagues were able to isolate the separate chains of IgG antibody in an undenatured form and relate them to the
0167-4919/85/$02.00
products of papain digestion. This allowed the proposal in 1962 of the now familiar four chain structure of IgG antibody. Amino acid sequence studies by Rod's group on the heavy chains from two h u m a n pathological IgGs and from pooled normal rabbit IgG, together with earlier studies by other laboratories on the light chains, provided evidence for the presence of variable and constant regions in the chains of IgG antibody. These structural studies helped solve the problem of how antibodies could recognize a vast range of different antigens yet react in a constant way with the molecules that triggered effector function subsequent to antibody binding. For his role in this work Rod was awarded the Nobel Prize for Physiology or Medicine jointly with Gerald Edelman in 1972. His move to Oxford University in 1967 as Whitley Professor of Biochemistry meant that he became heavily involved in teaching, administration and scientific committee work, yet he still managed to find time to successfully direct research in the M R C Immunochemistry Unit. His practical and direct approach to research was a feature throughout his career, as was his skill at stimulating and influencing the research of an international array of students, post-doctoral workers and visitors on sabbatical. All of these people felt a great respect and affection for Rod and valued the time spent in his laboratory. Much of his work at Oxford was involved with the mechanism by which antibody-antigen aggregates interacted with, and activated, the serum complement system and also with the detailed structural analysis of many of the complement components. In 1968-69 the Valentine and Green bivalent DNPhapten-anti D N P antibody system was used to show that well defined IgG complexes of tetramer size, or higher, efficiently bound and activated the C1 complex. Further work on IgQ, in the period 1971-73, allowed the characterization of Facb (fragment-antigen and complement binding) from plasmin digested IgG and helped define the CH2 domain as being the C 1 binding region. He then turned his attention directly to the complement system itself, and structural and functional studies on the subcomponents C 1q, C 1r and C ls occupied much of his interest during the period 1971-78. These studies included the proposal of a molecular model for the unusually shaped C l q molecule and a mechanism by which the C1 complex interacts with aggregated IgG to bring about activation of the proenzymes C l r and Cls. The activated C 1 complex enzymatically splits and activates C4, and an
Immunology Today, vol. 6, No. 10, 1985 interest in the functional role of C4 was central to Rod's personal research during the period 1978-85 which involved: sequencing the complex three chain protein; study of the covalent binding of activated C4 to the Fd region of IgG antibody; the demonstration that the different C4A and C4B types of C4 showed preferential binding to protein and polysaccharide, respectively; isolation of cDNA and genomic clones of C4 and studies on the genetics of C4. His group were also involved in work, at the protein and DNA levels, on C2 and factor B as well as C4, and the description and alignment of these Class III genes on chromosome 6 in the human M H C region in Nature (1984) was a highlight in his recent research. As more data on C4 accumulated, the possible role that allelic forms of C4A and C4B might play in determining an individual's susceptibility to autoimmune-type disease
291 became a major interest. It was remarkable that his research activity as he neared 'retirement' appeared to be increasing rather than decreasing. In the last few years he had been a prolific writer of articles and reviews and they all bore his characteristic clear, direct and brief style. He had a great ability to grasp quickly the essential points in a complex problem, be it scientific or administrative, and make a rapid assessment and decision. Throughout his career he received many prizes and honours, the most recent being the Companion of Honour awarded earlier this year, and he held many influential posts. However, one which gave him particular pleasure was appointment as a Curator of the Botanic Gardens at Oxford. His interests in gardening, bee keeping and other rural pursuits were carried out at his farmhouse where often an unsuspecting post-
doc would find himself engaged in some aspect of forestry or a wall-rebuilding programme. His relaxation away from Oxford was hill walking and he was very knowledgeable about the testing long walks and climbs throughout the U K and Continent. He and Julia had a knack of making the members of his Unit and visitors feel like one big family and the warmth of this feeling was well illustrated in July this year when many of his past co-workers gathered to form p a r t of a large audience which attended the Biochemical Society Symposium and Dinners held in his honour. It is a privilege to have been the friend and colleague of an outstanding scientist who had such a fine personality; he will be greatly missed. [~ KEN REID
M R C Immunochemistry Unit, Oxford, UK.
