Moore (Moore), Stanford

September 4, 1913, Mr.. - August 23, 1982
American biochemist Stanford Moore was born in Chicago (Illinois), in the family of John Howard Moore and Ruth (Fowler) Moore. Shortly after his son's birth parents M. moved to Nashville (Tennessee), where his father taught law at the University Vanderbiltskom. M. grew up in a family where there was an atmosphere that encourages intellectual pursuits, and soon showed an interest in chemistry, and his teacher in high school contributed to the development of this interest. Entering in 1931. in Vanderbiltsky University, M. fluctuated between chemistry and aeronautical engineering, but after studying the molecular structure under the leadership of Arthur Ingersoll opted for organic chemistry.
Received in 1935. Bachelor of Arts degree summa cum laude (with highest praise. - Lat.), M. was awarded a scholarship of the Scientific and Wisconsin Alumni Research Foundation, through which he was able to continue their studies at the University of Wisconsin. Here he wrote a work under the guidance of Karl Paul Link, who had recently worked in Europe, together with Fritz Pregl over microchemical methods to establish the atomic structure of organic compounds. For his thesis on the characteristics of carbohydrates and derivatives of benzimidazole, M. in 1938. received his doctorate.
This work M. was so great, . Link recommended that the young scientist to the German chemist Max Bergman, . shortly before arrived in the U.S., . to work in the Rockefeller Institute for Medical Research (now Rockefeller University) in New York,
. Bergman, who in his time spent as a research assistant to Emil Fischer, was considered one of the most eminent scientists in the field of protein chemistry. At that time, little was known about the structure of these extremely large organic molecules. In accordance with the previously prevailing view, which was first suggested by Fisher in 1908, it was believed that proteins are composed of amino acid strands bound in a polypeptide chain. At the invitation of Bergman M. began in 1939. work in the Rockefeller Institute of the method of determining the amino acid composition of proteins. One of his colleagues on the topic was an American biochemist William X. Stein.
When in 1941. The United States entered World War II, M. Rockefeller took a sabbatical of Wireless and served as a junior officer in the administrative work of the Office of Research and Development U.S.. Later during the war he was sent to the operational research department of the armed forces in Hawaii.
When the end of the war, in 1945, M. returned from the army, Bergman died, and the future, awaiting a scientist at Rockefeller Institute, it seemed highly uncertain. However, the director of the Institute, Herbert C. Gasser suggested that M. Stein and resume previous work on quantitative analysis of amino acids. Having at its disposal a laboratory, two scientists began to research. During the war years there has been some progress in the separation and purification of proteins, . in particular by first used in the field of biochemistry method of paper chromatography (the separation of complex mixtures by percolation through the absorbent) British scientists Archer Martin and Richard Singh,
. Martin and Singh found that after cleavage of the polypeptide chain into its constituent amino acids, they can sort through the amino acid characteristic speed with which they move through a special filter paper. At the same time, the English chemist Frederick Sanger began applying the method of paper chromatography to determine the types of amino acids and their quantitative ratio in insulin.
. Despite the fact that the new application method of paper chromatography opened up the possibility of obtaining useful data, M
. and Stein have been looking for the method of separation, which would provide more information about each of the acids. They stopped on the method of column chromatography, in which the solution to be analyzed is passed through the tube, which is placed a substance absorb various molecules with different speeds. Thus, the analysis can be seen as clear bands in the adsorption nozzle columns. Passing solutions of amino acids through the column with the attachment of potato starch, M. and Stein in 1948. first received positive results. However, this process takes about two weeks, and scientists have begun to seek more effective method.
In the early 50-ies. M. and Stein turned to a method of ion exchange chromatography, in which ion exchange resin sort out the ions according to their electric charges and sizes. This method is not only possible to expedite the analytical process, but also provided a clearer division than the method of column chromatography, using starch. Combining the two methods, M. and Stein conducted an analysis of amino acids that make up different proteins.
In 1950, Mr.. M. interrupted this work and first spent 6 months at the Free University of Brussels, and then another 6 months in England, working with Frederick Sanger at Cambridge University. After returning to the Rockefeller Institute, he once again in collaboration with Stein, he turned to the study of ribonuclease - the enzyme, or an organic catalyst that promotes the cleavage of ribonucleic acid. Another 30-ies. American chemists, James B. Sumner and John X. Northrop came to the conclusion that enzymes are proteins. Their structure however was known to very few. M. Stein and take up a fixed relationship between structure and function of ribonuclease.
. Chicago firm myasoupakovochnaya 'Incorporation Armor' secured M., Stein and their colleagues samples for analysis, and they proceeded to further purification of bovine ribonuclease by ion exchange chromatography
. They split the polypeptide chain of the highly pure enzyme preparation of land, divided the plots with the help of chromatography and identified were present in each of these amino. This process has become even more effective when in 1958. M. Stein and Darrel Spekman developed an automatic method for amino acid analysis, which later became permanently used for research in the field of biochemistry of proteins.
By 1960, Mr.. This group of scientists found a complete sequence of alternating amino acids of ribonuclease. It was the second set of protein sequences and the first of the sequences of enzymes. With their findings M. and Stein were able to identify the location and composition of the components of the active center of ribonuclease, which catalyzes the cleavage of RNA. After 1968. as a visiting professor of medical sciences in medical school Vanderbiltskogo University, M. returned to the Rockefeller Institute, where he and Stein controlled analytical studies deoxyribonuclease - an enzyme that breaks down deoxyribonucleic acid.
In 1972. M. and Stein was awarded half the Nobel Prize in Chemistry 'for their contribution to clarifying the relationship between chemical structure and catalytic action of the active center of ribonuclease molecule ". The second half of the prize was awarded to Christian Anfinsenu for work related to this topic. In his opening speech on behalf of the Royal Swedish Academy of Sciences BG. Maelstrom stressed that the understanding of the catalytic action of the enzyme depends on establishing the location of its active site. 'Through these studies, - he said, M. and Stein managed to create a detailed picture of the active site of ribonuclease long before they were installed three-dimensional structure of this enzyme '. In his Nobel lecture M. and Stein stated that 'very few of the macromolecules can speak with such detail, with what can be described by a molecule of ribonuclease, or hemoglobin. Such knowledge is the relationship between structure and function is fundamental for a rational approach to the complex synergy of living systems'.
After receiving the Nobel Prize M. continued his studies of enzymes in the Rockefeller Institute. Suffering from amyotrophic lateral sclerosis - a progressive disease of the central nervous system, the scientist August 23, 1982, Mr.. committed suicide at his home in New York at the age of 68 years.
M. was a man of high growth. He never married, gave himself entirely to research in the field of biology, firmly believing in the benefits that it brings. 'Knowledge of human rights - he said at the time when he was awarded the Nobel Prize - has even higher priority in the research, rather than man's knowledge of the universe'.
In addition to the Nobel Prize, M. and Stein received an award for achievements in the field of chromatography and electrophoresis (1964) and Theodore William Richards Medal (1972) American Chemical Society. M. was the holder of honorary degrees from universities in Brussels and Paris. He was a member of the American Association for the Advancement of Science, U.S. National Academy of Sciences, the American Chemical Society, American Society of Biological Chemistry and the American Academy of Arts and Sciences.