Hugo Theorell (Theorell), Hugo

July 6, 1903, Mr.. - August 15, 1982
Swedish biochemist Axel Hugo Theodor Hugo Theorell was born in Linkoping, the second of three children Tyure Hugo Theorell, a military surgeon, and Armida (Bill) Hugo Theorell. T. Dam, the excellent pianist who often accompanied her husband, a talented singer, instilled in the boy a love of music.
At the age of 3 years Hugo polio. Although the disease had been paralyzed left leg, produced after six years of operation to transplant the muscles gave him the opportunity to move. During convalescence, he learned to play the violin and by enrolling in the public secondary school in LinkцІping, became the conductor of the student orchestra, and was also chairman of the school of scientific society. In the summer of 1920,. T., dreaming to become a civil engineer, trained engineering at the Swedish railway. The following year, after graduating from high school, however, he decides to follow in the footsteps of his father and take up medicine.
In 1921, Mr.. T. enters the Karolinska Institute in Stockholm, he completes a training program for three years and in 1924. received a Bachelor of Medicine. After spending the summer at the Pasteur Institute in Paris, where he studied bacteriology, T. returned to Stockholm, where he was appointed assistant in medical chemistry at Karolinska Institutet. One of his first investigations was to study the influence of lipids (fats) in the newly developed clinical test - erythrocyte sedimentation rate (red blood cells), or ESR. This work showed that lipids contribute to the reduction of ESR. At the same time T. to refine electrophoresis - laboratory method, . used for separation of plasma proteins (albumin and globulins), . which he later used for isolation and purification of enzymes and coenzymes (resistant to heat, . water-soluble components of enzymes),
. After receiving the rank of professor in 1928. T. thesis on plasma lipids (fatty acids) and received in 1930. Doctor of Philosophy.
The following year he married Margaret Elizabeth Eline Ahlenius, pianist, has also made concert harpsichord music, which was trained to play musical instruments with one of the sisters T. Stockholm. The couple a daughter and three sons. During the honeymoon T. and his wife traveled on bicycles in England and then went to Paris where he met the harpsichordist Wanda Landowska. While his wife for five months studied music with Landowska in Paris, T. returned to the Karolinska Institute, where he worked as a doctor and gave lectures on biochemistry.
. At the same time he continued to study the physicochemical properties of myoglobin contained in muscle tissue and consisting of the protein part of the - globin and non-protein groups - a topic that was first discovered in 1897
. scientists of Karolinska Institute. As with hemoglobin, the oxygen carrier in red blood cells, myoglobin stores oxygen in the muscles of animals and humans.
While it was not clear whether the myoglobin and hemoglobin molecules are identical, and T. intended to carry out experimental work to resolve this problem. First, he identified a protein of myoglobin ultracentrifugation techniques (high-speed rotation in the centrifuge) and electrophoresis (movement of colloidal particles under the influence of an electric field). Then determine the physical and chemical characteristics of this protein, including the rate of sedimentation (deposition), diffusion, affinity for oxygen and the influence of pH on the affinity for oxygen. Finally, he compared the characteristics of the two molecules, and thus demonstrated that myoglobin and hemoglobin are not identical. However, he did not accurately determined that the molecular weight of myoglobin is half the mass of hemoglobin. (Later it was proved, . that the molecular weight of myoglobin is one-fourth of the mass of hemoglobin.) lower molecular weight explains the excretion of (separation) of the kidneys with myoglobin myoglobinuria, . state, . at which myoglobin is detected in the urine.,
. In 1932, Mr.
. T. appointed associate professor of medicine and physical chemistry at Uppsala University, . in the next two years, he - the Rockefeller Foundation Fellow at the Institute of Cell Physiology, Kaiser Wilhelm (now - Max Planck Institute) in Berlin,
. There, in the laboratory of Otto Warburg, he performed experiments for the isolation and identification of enzymes catalyzing cellular respiration or cellular oxidative reactions. By that time, when T. began the study of oxidative enzymes, biochemical model for biological oxidation and bioenergetics only created. In XIX. French physiologist Claude Bernard discovered glycogen in liver cells of experimental animals, as Louis Pasteur and other researchers have described the metabolism of glycogen and glucose in living cells.
. Glycogen, complex carbohydrate, is a form of storage of the main source of cellular energy - glucose - in the cells
. Glycogen and its cleavage product (glucose) are metabolized by one of two possible biochemical pathways: aerobic glycolysis, which requires the presence of oxygen, or anaerobic, occurring in the absence of oxygen,. In the latter case, glucose is converted into lactic acid, or lactate. The aerobic metabolism of glucose the way is a more natural mechanism for generating cellular energy than anaerobic.
. Albert Szent-Gyorgyi discovered, . that the oxidation of carbohydrates to carbon dioxide and water is catalyzed by certain enzymes from the group of carboxylase and oxidation processes use oxygen as the accession, . and removal of hydrogen and electrons, . recovery,
. By the mid 30-ies. is clear, . that the conversion of pyruvate (salt or ester of pyruvic acid) to carbon dioxide and water is a cyclical process, . in which the formation of energy-rich molecule adenosine triphosphate (ATP), . main source of energy for various biochemical processes of cells,
. T. interested cytochrome C, enzymes catalyzing oxidation reactions on the surface of mitochondrial 'power plants' cells.
Returning in 1935. in Stockholm, T. continued his studies of cytochrome C. This year he shared the crystalline cytochrome C into two components: coenzyme (catalyst) and apoferment (pure white), which together provide for oxidation reactions. Since its establishment in 1937. Medical Nobel Institute T. there was appointed professor and head of the Department of Biochemistry. With one of the staff, he visited laboratories in Europe and studied their technical equipment, to organize the most advanced research facilities in the walls of the newly created but not yet built the Institute. The outbreak of World War II delayed further work on his project. Although the neutrality of Sweden made it possible for T. further research, collaboration with foreign scientists has been limited.
In 1939, Mr.. T. spent three months in the U.S., studying the biochemistry of proteins with Linus K. Pauling at Caltech in Pasadena. Upon his return to Stockholm, he again focused on the biochemistry of hemoprotein, . especially on three-dimensional spatial relationship between the heme (non-protein, . insoluble, . containing iron protopofirinovoy part of hemoglobin), . protein components of cytochrome C and submolekulyarnymi mechanisms of biological redox reactions,
. During the war, he also studied another group gemoproteinovyh enzymes belonging to peroksidazokatalaznoy system. Peroxidase, which are oxidative enzymes are found in liver cells, and also involved in plant respiration.
After the war, the T. purified and obtained in crystalline form myoglobin from urine and heart muscle of two brothers who died from paralytic miolobinurii, a disease characterized by myopathy and the presence of myoglobin in the urine. During these years of research he and his colleagues on the basis of new biophysical techniques have developed experimental methods of study of hemoprotein, . that require relatively small amounts of biological material and were significantly improved compared with existing ones.,
. Medical Nobel Institute was opened in Stockholm in 1947, partly thanks to the support of the Rockefeller society and the National Institutes of Health USA
. Since T. not sought to teaching, he organized the work in research laboratories, according to their scientific interests. In particular, he directed the research of a number of prominent scientists, including Suna Bergstrema.
In the late 40-ies. T. in collaboration with Brighton Chance University of Pennsylvania drew attention to a group of oxidative enzymes, alcohol dehydrogenase, existing in various forms. Alcohol dehydrogenase - an enzyme that catalyzes the oxidation of alcohol (ethanol) in the aldehyde (acetaldehyde) in liver cells. Since T. Chance, and determined the sequence of reactions in this process, the mechanism of these reactions was named the mechanism Hugo Theorell - Chance's.
Nobel Prize in Physiology or Medicine 1955. was awarded to T. 'for their discoveries concerning the nature and mechanism of action of oxidative enzymes'. In his Nobel lecture with the presentation of awards T. described the ultimate goal of studies of enzymes as 'filling the yawning gap between biochemistry and morphology'.
In the 60-ies. and in the early 70-ies. T. perform administrative duties in the Central Fund Society Wenner-Green, engaged in the financing and organization of research scientists invited to Stockholm. After the departure of T. of the Karolinska Institute in 1970. Symposiums Wenner-Green on redox enzymes were performed in his honor.
Known among his colleagues as a kind, friendly man with a great sense of humor, T. many years was chairman of the Stockholm Philharmonic Society. Once transferred in 1974. stroke, his health began to deteriorate, and after two years of T. abdicated its responsibilities in the Wenner-Green Center. During the trip to the island of Luster in the summer of 1982. He died at the age of 79.
Awards T. include the Paul Karrer Medal in Chemistry University of Zurich, Scheele Medal of the Association of German pharmacists, medal Ciba Biochemical Society of London, a commemorative medal in honor of the 150 anniversary of the Karolinska Institute. He was a member of the Swedish Association of Chemical, . Swedish Society of Physicians and Surgeons, . Royal Swedish Academy of Sciences, . International Biochemical Society, . Royal Danish, . Norwegian and the American Academy of Arts and Sciences, . American Philosophical Society and the Royal Society of London,
. He was awarded honorary degrees from universities in Paris, Pennsylvania, Kentucky, Michigan, and Brussels.