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Lipman (Lippmann), Fritz

( German-American biochemist and Nobel Prize in Physiology or Medicine, 1953)

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Biography Lipman (Lippmann), Fritz
June 12, 1899, Mr.. - July 24, 1986
German-American biochemist Fritz Albert Lipmann was born in Koenigsberg (now z. Kaliningrad) at Gertrude (Lahmanski) Lipman and Leopold Lipmann, lawyer. Under the influence of his uncle, who was a pediatrician, L. in 1917. began to study medicine at the University of KцTnigsberg. At the end of the First World War, he spent several months in the army medical troops, and then continued his education in Munich and later at Berlin University, which awarded him in 1922. medical degree for a thesis on the colloidal chemistry. L. another three months left in Berlin, passing through an intensive three-month course in biochemistry, then received a grant for research in pharmacology at the University of Amsterdam (Netherlands). Deciding to become a biochemist, L. entered the University of KцTnigsberg. In 1927, Mr.. for a thesis on the biochemical reactions of muscle cells L. the University of Berlin received his doctorate in chemistry.
During the next two years he worked as an assistant to Otto Meyerhof in the Biological Institute of the Kaiser Wilhelm in Berlin. When in 1929. Meyerhof moved to the Institute for Medical Research in Heidelberg, Kaiser Wilhelm, L. followed him. In Heidelberg, L. acquainted with Otto Hahn - a specialist in nuclear physics, as well as biochemists Otto Warburg and Hans Krebs.
By the mid 20-ies. Scientists have developed a general scheme of cellular carbohydrate metabolism. It was found that carbohydrates, glycogen and glucose is threatened by chemical cleavage, both by oxidation (aerobic glycolysis, or respiration), and fermentation (anaerobic glycolysis). In the first case of glucose (a molecule with 6 carbon atoms) is converted into a molecule of pyruvic acid with 3 carbon atoms, which is then oxidized to carbon dioxide and water. In anaerobic glycolysis pyruvate transformed into lactate (as a molecule with 3 atoms of carbon). Meyerhof showed that a small but significant part of lactate, produced by active muscle cells, is oxidized further to carbon dioxide and water.
Like Meyerhoff, L. was interested in clarifying the mechanisms by which living cells produce and utilize energy. He found that sodium fluoride inhibits the oxidation of lactic acid. L. also studied the biochemistry of creatine phosphate (phosphocreatine), the splitting is closely associated with muscle contraction, as lactic acid. In 1931, Mr.. L. returned to the Kaiser Wilhelm Institute for Biology in Berlin as assistant to Albert Fischer, who taught him to grow fibroblasts (cells of fetal tissue) in culture in vitro - a very useful method for studying cellular metabolism.
. After his older brother, actor, A
. acquainted with the literary and theatrical life in Berlin. It is in these areas at fancy-dress ball, he met with American prison Elfredu M. Hall, whom he married in 1931. In the same year the couple moved to New York, where, having received the Rockefeller Foundation grant, L. with a chemist P.A. Livigno studied the phosphorylation of proteins in the Rockefeller Institute for Medical Research (now Rockefeller University).
In 1932, Mr.. L. again joined Fisher in the new laboratory of the Biological Institute, Carlsberg Foundation in Copenhagen (Denmark). Over the next 7 years he has studied how cells produce energy to carry out biochemical reactions necessary to sustain life. He found that in the presence of oxygen, anaerobic glycolysis is suppressed. For the analysis of this phenomenon, called the Pasteur effect, L. studied the oxidation of pyruvate (ester or salt of pyruvic acid, an intermediate product of the metabolic process). With the enzyme system derived from the bacterium Lactobacillus delbrueckii, he showed that the conversion of pyruvate to acetate is completely independent of inorganic phosphate and leads to the formation of phosphorylated forms of acetate - acetyl. L. came to the erroneous conclusion that acetyl is chemically active form of acetate, which combines with oxaloacetate, forming citric acid in the first link in the Krebs cycle - chain reactions of metabolism of carbohydrates and fatty acids.
In the late 30-ies. Nazi Germany extended its sphere of influence and in Denmark. Realizing that being a Jew, he could not return to Germany or to stay in Denmark, L. with his wife in 1939. emigrated to the United States. There he received the position of researcher in the Department of Biochemistry, leadership Vincent du Vigneaud, the Medical College of Cornell University (New York). He remained at Cornell until 1941 and then became a Fellow of Surgery, Harvard Medical School and Massachusetts General Hospital in Boston. Two years later, L. became research associate and then in 1949. - Professor of Biochemistry at Harvard. In 1944, Mr.. He became an American citizen, in the following year the couple Lipman, a son.
A study of cellular metabolism L. in 1941. suggested that the main source of energy to maintain metabolic reactions in living cells is adenosine triphosphate (ATP) - the central compound of the phosphate group making up the molecular structure of the nucleotide. Chemical bonds formed by this phosphate group, supplying energy, recyclable cells of the human body. However, until the opening of L. and his colleagues coenzyme A in 1945. was not clear how the ATP releases the cellular energy. After the isolation and synthesis of this catalyst L. showed how the ATF is helping to transform the energy of phosphate bonds in other forms necessary for the body of chemical energy. This discovery has made an important addition to the transcript of the Krebs cycle, during which food is transformed into physical energy in the cell. Coenzyme A is in all living cells - plants, animals and microorganisms.
L. was awarded the Nobel Prize in Physiology or Medicine 1953. for the 'discovery of coenzyme A and its importance for the intermediate stages of metabolism'. Along with awards won Hans Krebs. In the opening speech on the occasion of awarding Eric Hammarsten of the Karolinska Institute said: 'This - the recognition of deep and important achievements in the research functions of a living cell'. Addressing to the AL, Hammarsten continued: 'You have overcome a major obstacle, clearly demonstrating the mechanism of widespread reaction and simultaneously opening a new way of energy transfer in a cage'.
In 1957. L. became Professor of Biochemistry, Rockefeller University. There he devoted himself to the study of unusual phosphate compounds, . such, . as karbamoilfosfat, . structure of cancer cells, . thyroid hormone and its role in the regulation of energy exchange in the body, . processes, . occurring in the intermediate phases of metabolism,
. After receiving an honorary professor of Rockefeller University in 1970, L. until the last days of his life remained an active researcher.
L. died July 24, 1986, Mr.. in Pouskipsi (New York).
L. was a member of the National Academy of Sciences, the American Society of Biochemistry, Garveevskogo Society, the American Philosophical Society, as well as foreign member of the Royal Society of London. He was awarded the Carl Neuberg Medal of the American Society of European Chemists (1948), the National Medal 'For his scientific achievements' of the National Science Foundation (1966). He was awarded the Mead Johnson Award of the American Academy of Pediatrics (1948), . honorary degrees from universities in Paris, . Aix - Marseille, . Chicago and Copenhagen, . and Harvard, . Rockefeller University and the Albert Einstein College of Medicine.,


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