Porter (Porter), Rodney R.

October 8, 1917, Mr.. - September 7, 1985
English biochemist Rodney Robert Porter was born in Newton-le-Villouse, located in the historic area of Lancashire, England, the son of Joseph L. Porter, an employee of the railway, and Isabelle Porter. Before entering the University of Liverpool, Rodney attended school in Aston-in-Meykfild. In 1939, Mr.. He graduated with honors from the university, a Bachelor of Science in Biochemistry. The following year he was drafted into the army, served in the Royal Engineers and Signal Corps, took part in the hostilities in North Africa and Italy. In January 1946,. He was discharged from the Armed Forces with the rank of Major.
After demobilization P. went to Cambridge University to study biochemistry led by Frederick Sanger. There, he read a book by Karl Landsteiner 'specificity of serological reactions' ( 'The Specificity of Serological Reactions'), which described the nature of antibodies, this work aroused the interest of P. to study their structure and function, continues unabated throughout his life. Antibodies represent a class of proteins of blood plasma related to the immunoglobulins (Ig). For many centuries it was known that there are some diseases (including measles and smallpox), which man can perebolet only once. If someone is suffering from this disease, it became immune to it and never got sick again. In 1890, Mr.. Emil von Behring demonstrated that immunity is due to antibodies that interact with pathogens or the emission of toxins, making them so inactive. Any substance that stimulates the formation of antibodies, called an antigen.
The antibodies are so specific that immunity to one disease is not accompanied by the emergence of resistance to other. Job Landsteiner in the 20's and 30-ies. showed that a large number of substances can act as antigens and the body is able to produce millions of different, but highly specific antibodies. When P. began to study antibodies, their structure was known to few. It was believed that all Ig molecules have the same size and structure. 'This combination of distinct specificity of the antibodies with the fact that it seemed almost a homogeneous group of proteins that surprised me, and continues to amaze', - said P. later.
To find out how the antibodies combine a variety of functions with uniform structure, P. first tried to destroy the purified Ig molecules by various enzymes. The most important type of Ig in the blood - IgG - consisted of more than 1300 amino acids. IgG molecules were too large, . that they can be studied by Sanger, . used to determine the sequence of amino acids in a protein molecule (the work of Sanger at the time dealt with insulin, . which contained only 51 amino acids),
. However, there was evidence that the active site of antibodies - part of the molecule that actually interacts with the antigen - much less. P. hoped that by selecting the appropriate enzyme, it will be able to allocate part of antibodies, available in size for research, but at the same time containing the active center. Initial studies P. shown that papain, an enzyme juice papaya (melon tree) may be divided into fragments of IgG, which amounted to 1 / 4 of the antibody molecule. For this work he had in 1948. received his Ph.D. from Cambridge University.
P. continued to investigate the antibodies in the laboratory Senger during the year before the transition in 1949. the National Institute for Medical Research in Mill Hill (London). Although he was accepted as a biochemist in microbiological research group, he continued to study antibody. During 50-ies. he improved methods of purification of protein mixtures and used some of them, to show that not all IgG molecules are identical, although these differences are small compared with the diversity of their activity.
Success came in 1957 when P. earned a net instead of crude papain enzyme preparations, which he used in Cambridge. Repeating his earlier experiments, he found that pure papain cleaves IgG molecule into three fragments (each of about one-third of the entire molecule) of two different types of. One of the fragments was called 'crystallization', or Fc-fragment. Even the most refined at the time IgG is not crystallized, tk. was a mixture of several different antibody molecules. However Refragment crystallized, indicating its similarity in all the molecules of IgG. Because the Fc-fragment did not contain the active center, the ability to bind antigens remained in the other two-thirds of the antibody molecule, the two 'antigen-binding fragments', or Fab-fragments.
P. published the results of his research in 1959. The following year, Gerald M. Edelman and his team managed to split the IgG method, which does not break the connection in the protein molecule between amino acids, as does papain, and shares some amino acid chains. In 1960, Mr.. P. moved to London and continued his work in the medical school at the Hospital of St.. Mary, where, Edelman repeated the experiments under different conditions, he proved that his methods split the molecule at right angles to the explosions caused by papain. P. summarized his results with the data of Edelman in 1962. proposed the first satisfactory model of the structure of IgG. Although she did not give an answer to a question, . What accounts for the presence of antibodies such a broad spectrum of activity, . however, . assuming, . that Fab-fragments are composed of parts of two different amino acids, . model formed the basis for more detailed biochemical studies.,
. During the 60-ies
. Many researchers in various academic institutions have tried to explain the function of antibodies by means of chemical terms. In these surveys the leading role played by P. and Edelman, who by their personal involvement inspired other scientists, organizing a series of 'informal workshops on the antibodies' to exchange ideas. P. and his colleagues have conducted numerous studies of the structure of individual molecules of IgG, while the group Edelman determined the complete amino acid sequence in one molecule of IgG. Their findings were published in 1969
P. and Edelman shared the Nobel Prize in Physiology or Medicine 1972. 'for the discovery of the chemical structure of antibodies'. P. gave his Nobel lecture "Structural studies of immunoglobulins' ( 'Structural Studies of Immunoglobulins'). By this time the main question about the diversity of antibodies was not in their structure, . in the mechanism of their formation, he was allowed only in the late 70's., . when the development of recombinant DNA technology has enabled scientists to directly study the genetic aspects of antibody synthesis.,
. In 1967
. P. was appointed professor of biochemistry and head of the department of biochemistry at Oxford University, where he continued research in the field of immunochemistry. In search of confirmation of predictions Macfarlane Burnet on the location of antibodies on the surface of cells antitelprodutsiruyuschih P. developed ways of tagging specific cell surface receptors. He also studied the chemical and genetic aspects of complement, a group of blood proteins (open Jules Bordet), which bind to Fc-fragment of Ig and participate in many important immunological reactions.
A month before the resignation of Oxford P. died in a car accident in Winchester. Since 1948. married to Julia France-New York, they had two sons and three daughters.
In addition to the Nobel Prize, P. received an honorary award Gardner Fund (1966) and the Ciba Medal Biochemical Society (1967). He was a member of the Royal Society and a foreign member of the U.S. National Academy of Sciences.