Edelman (Edelman), Gerald M.

genus. July 1, 1929
American biochemist Gerald Maurice Edelman was born in New York, the family physician Edward Edelman and Anna Edelman (Friedman). After public school in New York, he enrolled at Ursinus College in Pennsylvania and in 1950, Mr.. received a bachelor of science degree in chemistry. Then E. entered medical school at Pennsylvania University and in 1954. received a medical degree. Then within a year he worked as a doctor in central Massachusetts hospital. Since 1955, enlisted in the armed forces of the United States, he worked as a General Practitioner in the garrison hospital in Paris.
In 1957. E. demobilized and decided to leave the medical career for the sake of research in the field of biochemistry. He began working on his thesis at Rockefeller University under the leadership of Henry Kunkel, a biochemist who studied the structure of antibodies. Antibodies, open Emil von Behring in 1890 - is a serum protein belonging to the group of immunoglobulins (Ig). Ig molecules can interact with bacteria, viruses and toxins and inactivate them, so they play a crucial role in humoral immunity of the organism. Antibodies are characterized by an unusual combination of biochemical properties. Karl Landsteiner found that the organism can be worked out millions of different antibodies, each of which interacts with a strictly defined substance or antibody. However, the chemical structure of antibodies is so similar, that is practically impossible to distinguish from the blood of certain antibodies. Kunkel and his colleagues wanted to determine why the molecule Ig at the same time so similar in structure and have functional differences.
. Research structure of antibodies have been hampered by the fact that there were no methods for their treatment and their molecules are very large compared with other proteins
. Chemical methods that existed in the late 50's. Not allowed to study such large molecules. E. believed that the structure and function of antibodies can be studied, Ig molecules are split into smaller fragments, while expecting that these fragments retain the ability to interact with antigens. In his doctoral thesis he examined the various ways of splitting molecules Ig. In 1960, Mr.. E. received his doctorate and stayed to work at Rockefeller University researcher and teacher.
Predecessors E., in t.ch. Rodney P. Porter, first split the antibodies on the functional subunits, came to the conclusion that the molecules of IgG, which accounted for most of the Ig molecules of blood, are formed by a single chain of 1300 amino acids. E. thought it unlikely that T. to. even insulin, comprising only 51 amino acids, consists of two chains.
. Because the chemical bonds that connect with each amino acid chain, is much weaker than those by which amino acids are connected within chains, these connections can be relatively easy to destroy
. In 1961. E. and his colleague, M. Pulik reported that they shared the IgG molecule into two components, which are now referred to as light and heavy chains. Repeating the experiments E. in other circumstances, Porter combined results with the data of own researches of functional subunits of IgG and in 1962. announced the deciphering of the basic structure of IgG molecule. Although Porter's model was of a fairly general nature, she played a crucial role as a kind of benchmark for special biochemical investigations.
When in the 60 g. began intensive work on the study of antibodies, Porter and E. organized work for the exchange of information between researchers through informal workers 'meetings for the antibodies'. They themselves studied proteins myeloma - a malignant disease-forming organs, characterized by the growth of plasma cells which produce Ig. One of the main difficulties in studying the antibody was that the natural Ig preparations usually contain a mixture of a large number of slightly differing molecular. In 1950, Mr.. Kunkel found that, since all the myeloma cells in a given patient usually occur from one cell precursor, these cells are the natural producers of homogeneous antibody. (It is this ability to produce homogeneous antibodies in addition to those antibodies that are commonly found in cancerous tumors, formed the basis of production technology of monoclonal antibodies, developed in 1975. George KцІhler and Cц?sar Milstein.)
In the early 60-ies. E., Porter, and their colleagues studied the sequence of amino acids in different chains of myeloma paraproteins. In 1965, Mr.. E. and his staff have taken, he said, 'absolutely insane venture - to examine all of the whole molecule, it was a terrible great work'. In an effort to find out how individual parts of the antibodies connected to each other, they have established a complete amino acid sequence of the molecule IgG myeloma. In 1969. This work was completed, the scientists found a sequence of 1300 amino acids forming the protein chain. At that time it was the biggest decoded amino acid sequence.
Model Ig Porter was particularly valuable because the active site antibody (ie. that portion that binds to the antigen) was formed as a heavy and light chains. This discovery led to a fundamental revision of the main reasons for the diversity of antibodies, namely the question of how to produce various antibodies. Interest in this subject in the 50-ies. steadily, as the study links between genes and proteins. In the human body can be shaped at least 10 million different proteins IgG, with 10 million active sites. If the antibodies, as well as other proteins that evolved in accordance with the theory of George I. Beadle and Edward L. Teytema 'one gene one protein', then the body would have existed 10 million. genes IgG and for other purposes, the DNA would simply not enough. Solving this problem, Macfarlane Burnet in the late 50-ies. suggested that antibodies are formed from the genes affected by mutations in the Ig-producing cells. However, if in accordance with Porter's model active sites of Ig formed from elements of two different amino acid chains, the existence of 10 million. genes coding for all antibodies is no longer necessary. This amount of antibodies can be formed by all possible combinations of 3 thousand. heavy and 3 thousand. light chains encoded by the corresponding genes. In 60 ... 70's.
. was a stormy debate between academics, . upholding the concept of the existence of individual genes for each of heavy and light chain, . and researchers, . who believed, . that there are only a few genes for heavy and light chains, . which mutate and form different proteins.,
. E
. did not agree with any of these theories, and in 1967. he and his associate Joseph Gelli proposed a new solution. By this time it was already known that each chain - heavy or light - is formed under the action of two genes, shifting and recombining in the development of antibody-producing cells. E. Gelli, and suggested that the diversity of antibodies is due to small errors in the process of recombination. However, although the concept was essentially correct, it is too much ahead of its time to become generally accepted that occurred in the late 70's. When techniques of genetic engineering allowed to directly study the genes encoding the antibody.
. In 1972
. E. and Porter was awarded the Nobel Prize in Physiology or Medicine "for discoveries concerning the chemical structure of antibodies'. In his Nobel lecture E. indicated that immunology is a particularly fruitful area for the scientist, t. to. 'she makes to generate unusual ideas, many of which are not so easily arise in other areas of science'. He predicted that "for this reason immunology have a marked impact on other biological and medical disciplines."
After receiving the Nobel Prize E. began to study other substances which, like the antibodies activate cells of the immune system. In addition, he in 1978. offered a fundamentally new theory of the functioning of the brain, which prompted his research in immunology. Fact, . that the immune response of the organism taken root in it a virus or bacterium is not 'teach' the immune system to, . how to synthesize the corresponding antibody, . but rather cause selection among the existing options for effective antibody; further in the body formed a clone of such antibodies,
. By analogy, E. suggested that the sensory stimulus does not induce a reaction in advance of certain brain cells and leads to the selection among 'competing' cell groups and relationships. Such representations correspond to the selection of Darwin's theory of evolution. An important requirement for the possibility of such selection is the diversity that E. contrasted relatively rigid biological structures capable of engaging only one and the same reaction to changing environmental conditions. The source of diversity in brain E. thought process of embryonic development.
In accordance with his point of view, genes determine the formation of embryonic tissues, but not in detail. Individual cells are not designed in advance for the formation of specific organs. Instead, certain genes are responsible for the formation of different types of intercellular cementing substance (several varieties of such substances were found E. These groups are sending signals that turn on or off 'tsementoprodutsiruyuschie genes', and thus to some extent regulate its further development. Different cell groups (which have different types of 'cement') form the border between them, and, as shown by E. and his colleagues, in groups, located on opposite sides of such boundaries, develop various cells. This process has been demonstrated in the laboratory of E., in experiments on the formation of individual feathers in the chick. Since the development of the cell depends on its location, history of development, environment, and possibly other factors, two of the embryo may not be identical, even in the case of twins with an identical set of genes.
Subsequently, E. determine how the initially flexible structure and organization of brain cells may be after the end of embryonic development and birth of a child to act as a system, learning through breeding. His theory is based on three main propositions: the embryo in the brain produced an extremely volatile individual system of relations between the cells, after the birth of this system is fixed, and each person is different, . but the stimulus may cause a reaction, . which involve certain combinations of bonds, and finally, . group of cells integrated into sheets (like road maps), . interacting with each other to perform a variety of higher brain function,
. His theory explains much of the enormous flexibility of the brain, . manifested in the ability to function in unusual situations and events, . as well as the failure of many researchers, . trying to find a specific structural substrate of these functions of the brain, . as a memory.,
. Since 1963, Mr.
. E. served as deputy dean for graduate school at Rockefeller University, and in 1966. became a full professor of the university. Since 1974, Mr.. He works as an Honorary Professor at Rockefeller University. He is a member of the Chief Executives Board Weizmann Institute and a trustee Solkovskogo Institute for Biological Studies.
In 1950, Mr.. E. married Maxine Morrison, in the family they have one daughter and two sons.
In addition to the Nobel Prize, E. was awarded Spencer Morris, University of Pennsylvania (1954), . Eli Lilly Award of the American Chemical Society (1965), . Memorial Prize Albert Einstein Yeshiva University (1974) and Buchman Memorial Prize for the California Institute of Technology (1975),
. He was a member of the New York Academy of Sciences, the American Academy of Arts and Sciences, the National Academy of Sciences, the American Society of Cell Biology and the American Society of Geneticists. He has honors at Pennsylvania State University, University of Siena, Ursinus College, Williams College and Gustavus Adolphus College.