Stein (Stein), William H.( American biochemist and Nobel Prize in Chemistry, 1972)
Comments for Stein (Stein), William H.
Biography Stein (Stein), William H.
June 25, 1911, Mr.. - February 2, 1980
American biochemist William Howard Stein (Stein) was born in New York. He was the second of three children, Beatrice (Borg), Stein and businessman Freda M. Stein. S. Lincoln was in high school - a progressive school at Teachers College, Columbia University. Being engaged in the penultimate and final year of school, he also attended classes at Phillips Exeter Academy in Andover (Mass.).
In 1929, Mr.. S. enrolled at Harvard University and 4 years later received a bachelor's degree in chemistry. He went on to study chemistry at Harvard, but in the first year of managed so poorly that he was on the verge of dropping classes. Instead, C. decided to switch to biochemistry and in 1934. moved to the location in New York, College of Physicians and Surgeons of Columbia University. Find here the incentives for intellectual activity, which he lacked, he said, in his words, 'a short time to learn an enormous amount of material'. For his thesis on amino acid content of protein elastin, in his 1938. was awarded a doctoral degree. Like other proteins, elastin is a large molecule composed of amino acids linked together in the polypeptide chain. Although the structure of elastin at the time was still unclear, the thesis with. was a step forward in the understanding of its components.
After obtaining his doctoral degree with. started working at the Rockefeller Institute for Medical Research (now Rockefeller University) in New York under the leadership of Max Bergmann, . which he later spoke as "one of the greatest experts XX century in the chemistry of protein ',
. At the Rockefeller Institute with. was determined in the same group with Stanford Moore: they should try to develop more effective ways of analysis of amino acids in proteins.
When the U.S. entered World War II, Moore was drafted. He was assigned to Washington, and C. and his colleagues at the Rockefeller Institute were working on related projects for the military objectives of the Office of Research and Development U.S.. In 1944, Mr.. Bergman died. However, after the war ended in 1945, director of the Rockefeller Institute, Herbert C. Gasser suggested that C. and Moore to continue previously initiated studies in the field of quantitative analysis of amino acids.
. By this time, they can already take advantage of the, . that has been opened which is of vital importance to the method of separation and purification of protein, . developed in 1944, . when the English chemist Archer Martin and Richard Synge first used the method of paper chromatography to solve biochemical problems,
. With this method, amino acids, which were split off from the peptide chain, separated from each other as they pass through a special filter paper with a characteristic and different for each speed.
. Despite the fact that the method of paper chromatography proved to be quite fruitful, he still did not provide such data on the number of amino acids, which was necessary with
. and Moore in their studies. English chemist Frederick Sanger invited them to apply the method of column chromatography, . where the solution to be analyzed is passed through the tube with the substance, . absorbing components of this solution at different speeds, . thus, . results of this absorption can be observed as clear bands in the adsorption nozzle columns,
. Applying a filter, potato starch, C. and Moore in 1948. first succeeded. However, the passage of amino-acid solution through the column took two weeks. To expedite this process, they were used as a nozzle exchange resins. These substances, which are sorted by their molecular ions electric charge and size, provides faster results and greater clarity than the nozzle of the starch.
By that time, when C. in 1954. became a full professor at Rockefeller University, he has already conducted an analysis of amino acids found in a variety of proteins. However, the main effort, he focused on the enzyme ribonuclease, one of the many thousands of organic catalysts that regulate chemical reactions in living organisms. Despite the fact that James B. Sumner and John X. Northrop in 30-ies. proved protein nature of enzymes, the molecular structure of the latter until the mid 50-ies. remained unclear. It was believed that the difference in their functioning reflects a difference in their molecular structure.
With. and Moore decided to establish a sequence of alternating amino acids of ribonuclease. Using the method of ion exchange chromatography, they were high-purity samples of this enzyme. After destroying the chemical bonds in the protein and a mixture of 15 peptides, they shared peptides, using the method of chromatography, and established a sequence of alternating amino acids, and in 1960. reported their findings. Due to their findings other researchers were able to Rockefeller University in 1967. reach a conclusion on a three-dimensional configuration of ribonuclease, thus confirming the prediction. and Moore about the location of the active center of this molecule.
In 1972. S. and Moore 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 Christian Anfinsen for research related to this topic. 'On the basis of the knowledge structure of large enzyme - said. and Moore in their joint Nobel lecture - will develop the fundamental principles of understanding how to 'plan' the nature of the catalysts are certain purposes'. And referring to the discoveries, . associated with hemoglobin, . which were made shortly before this, and follows from the results of their research, . Scientists suggested, . that 'a study done by the protein will promote practical outcomes'.,
. collaborated with Moore not only in the study of ribonuclease. Together they investigated the structure and function of pancreatic deoxyribonuclease - an enzyme that hydrolyzes (splits) deoxyribonucleic acid. Interest. to disseminate scientific information contributed to the fact that a scientist devoted much of his time 'the journal of biological chemistry' ( 'Journal of Biological Chemistry'), where from 1958 to 1961. worked as an editor, in 1962. was a member of the Editorial Board, from 1964 to 1968,. was deputy chief editor, and from 1968 to 1971. - Editor in chief.
In 1936, Mr.. S. married Foeb Hoksteyder. In the couple had three sons. In 1969. scientist seriously ill. Despite the fact that he developed paralysis and was confined to a wheelchair, C. retained a keen interest in research until the last days of life. He died on February 2, 1980, Mr.. In New York, pp colleague, with whom he worked all his life, Stanford Moore spoke of him as a 'seminal and brilliant biochemist. "
In addition to the Nobel Prize, C. and Moore received the award for achievements in the field of chromatography and electrophoresis (1964) and Theodore William Richards Medal (1972) American Chemical Society. In 1968 ... 1969. S. was chairman of the State Committee for Biochemistry, USA. He was a trustee of Montefiore Hospital and was a Medical Advisory Board of the Jewish University Medical School.