Du Vigneaud (du Vigneaud), Vincent( American biochemist and Nobel Prize in Chemistry, 1955)
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Biography Du Vigneaud (du Vigneaud), Vincent
May 18, 1901, Mr.. - And in December 1978
. American biochemist Vincent du Vigneaud was born in Chicago (Illinois) in the family of Alfred du Vigneaud, inventor and constructor of machines, and Mary Theresa (nee O'Leary) du Vigneaud.
. Primary education he received in the Chicago public schools
. By being very early interest in the sciences, the boy spent in home laboratory experiments in chemistry and physiology. In 1918, Mr.. he entered the University of Illinois, where he specialized in organic chemistry, and in 1923. received a bachelor's degree, and the next year - Master's degree in Chemistry for his scientific work devoted to the synthesis of drugs, having a local anesthetic and vasopressor (causing high blood pressure) effect. These early studies led him to what he later called 'nagging interest in the relationship between the chemical structure of organic compounds and their biological activity. "
Interest in du. Insulin was born after the lecture VK. Rose, read at the Department of Chemistry University of Illinois shortly after the discovery of insulin, Frederick G. Banting and John JP. Macleod. Later in du. recalled how he was "struck by the fact that the chemical structure of this compound may have such amazing properties described Rose. I never thought that insulin could ultimately prove sulfur compounds'.
In 1924, Mr.. In du. mainly worked in the Jackson laboratories of the company 'du Pont de Nemours' in Wilmington (Delaware), . then became an assistant, a biochemist at the Higher School of Medicine, University of Pennsylvania and in the laboratory of clinical chemistry at the Philadelphia General Hospital, . where he worked,
. In 1925, Mr.. he joined the faculty of economics livelihoods (in fact, Faculty of endocrinology and metabolism) in the newly established medical school of the University of Rochester.
At the University of Rochester in du. The chemical composition of insulin. Two years later he wrote, . that insulin, . apparently, . is a derivative of the amino acids cystine, . that sulfur, . found in insulin, . is in the form of disulfide bridges and that insulin, . likely, . a peptide (two or more amino acids, . linked together),
. Because the nature of the known 20 amino acids, the chemical structure of long peptides and proteins often very complicated.
In 1927, Mr.. In du. University of Rochester received a doctorate in chemistry. Through grants from the National Research Council, he went to medical school at Johns Hopkins at the Faculty of Pharmacy, where he managed to identify the amino acid cystine crystals of insulin. He also discovered that insulin contains only amino acids and ammonia, although ammonia, as was proved later, is a byproduct.
In 1928, Mr.. In du. went to Germany, in Dresden, in the laboratory of Max Bergmann, who once was a student of Emil Fischer, and is already a recognized authority in the field of chemistry of amino acids and peptides. Although Bergman invited him to become his assistant, du In. rejected this proposal, continuing his work with biologists George Bargerom from the University of Edinburgh (Scotland) and Charles Harrington of the University College of London University (England).
Upon returning du In. admitted to University of Illinois at the Faculty of physiological chemistry. In 1932, Mr.. He became a professor of biochemistry and head of biochemistry faculty at the Medical School of George Washington University in g. Washington (DC), which developed a training program in biochemistry for medical students. In addition, he conducted research on the possible relationship between gipoglitsemicheskim effect of insulin (decrease in blood sugar) and the presence of disulfide bonds of cystine. To check this, he synthesized peptides containing cystine, and examined them in the physiological experiments (samples) on insulin activity.
In 1936, Mr.. He and his colleagues synthesized Glutathione - tripeptide containing amino acids - cysteine, glycine and glutamic acid. Glutathione, found in all tissues of animals, acts as a reducing agent (electron donor). In 1937, Mr.. In du. published the final proof that all the sulfur of insulin contained in the amino acid cystine, and that the restoration of disulfide bonds of insulin glutathione or cysteine makes it physiologically inactive.
In the next year in du. became a professor of biochemistry and dean of the faculty of biochemistry at Cornell University Medical College in New York. There he continued his attempts to allocate, . purify and synthesize the hormones oxytocin (which stimulates uterine contractions during childbirth and causes the flow of milk from the female mammary glands) and vasopressin (which stimulates constriction of peripheral blood vessels and promotes readsorbtsii water in the kidneys, . t,
. e reduce the volume of urine). During the study of biological transmetilirovaniya (transfer methyl groups from one molecule to another), he and his colleagues found that the methyl groups are important factors in the diet. They also identified from liver tissue and milk biotin - a coenzyme that participates in cell respiration and demonstrated that it is identical and the structure and properties of substances, then known as vitamin H or coenzyme R.
. During the Second World War in du
. worked on the synthesis of penicillin - a fungal antibiotic, discovered in 1928. Alexander Fleming. However, only after the war, in 1946, he and his colleagues have developed a synthesis of fully penicillin.
In Du. and his colleagues continued their work on the allocation of oxytocin from the commercially available extracts of the pituitary and pituitary tissues of bovine and swine. They found that regardless of the source of oxytocin always contains eight of the same amino acids and causes the same biological effect. Sulfur content in oxytocin fully coincides with the number of such amino acids as cystine. In 1953, Mr.. In du. determined that oxytocin - a cyclic polypeptide, whose structure consists of pentapeptidnogo (five amino acids) of the ring and tripeptide side chain. System pentapeptidnogo ring dvadtsatichlennaya structure is closed disulfide bridges, has not been previously detected in the chemical structures of known natural compounds. In Du. and his colleagues were the first crystalline oxytocin, which is experienced by women for induction of labor, and proved that it is effective for clinical use. This was the first synthesis of the polypeptides of the hormone in conditions in vitro.
In 1955, Mr.. In du. was awarded the Nobel Prize in Chemistry 'for his work with the biologically active compounds, especially for the first time carried out the synthesis of polypeptide hormone'. In his Nobel lecture he told about the history of studies of these sulfur-containing peptides: 'From a series of experiments in the lab, just do not know what in the end will come. Moreover, we must be sure that you have formulated a goal and you feel a certain sense, to be outside the specific purpose sought by the '.
All these years in du. maintained close collaboration with both clinicians and specialists involved, like himself, the fundamental problems. From 1967 to 1975. He was professor of chemistry at Cornell University in Ithaca. He became a board member of the Rockefeller Institute for Medical Research, National Institute of Arthritis and Metabolic Diseases and the Research Council Institute of Health in New York. He also served as president Garveevskogo Society and American Society of Biological Chemistry and chairman of the Federation of American Societies for Experimental Biology.
In 1924, Mr.. In Du. married Zell Eon-Ford, with whom they raised a son and daughter. A tall man with a thin brush mustache, he liked to play bridge and ride on horseback. He died Dec. 11, 1978, Mr.. G. Skarsdeyle (New York).
Among other awards in du. Nichols is a medal of the American Chemical Society (1945), . Borden Award in Medical Sciences, . Osborne and Mendel Award of the American Institute of Nutrition (1953), . Charles Frederick Chandler Medal, Columbia University (1956) and Willard Gibbs Medal of the American Chemical Society (1956),
. He was a member of the U.S. National Academy of Sciences, the American Academy of Arts and Sciences, the New York Academy of Sciences and the American Philosophical Society.