Northrop (Northrop), John H.

July 5, 1891, Mr.. - May 27, 1987
American biochemist John Howard Northrop was born in Yonkers (New York), in the family of Alice Bell (Rich), and Isaiah, John Northrop, professor of zoology at Columbia University. Shortly before the birth of H. his father died: in the laboratory, where he worked, an explosion. The boy's mother was again teaching botany at Hunter College in New York. Thanks to her efforts in the curriculum of secondary schools, a new subject - the study of nature. In New York, N. graduated from the start and in 1908. secondary schools.
Attended Columbia University, the future scientist devoted much time to studying the chemistry and very few - of biology. In 1912, Mr.. He earned a bachelor of science and graduate studies in chemistry. During graduate school H. joined the fencing team of Columbia University, which in 1913. won the inter-university competition. In the same year, H. become a master of science and started writing his doctoral dissertation in chemistry, where he graduated in 1915. In the summer of that year, just before its completion, a young biochemist, worked as a prospector in Arizona.
Getting a scholarship provided by William Beyarda H. opportunity to work throughout the year at the Rockefeller Institute for Medical Research (now Rockefeller University) in Jacques Loeb, after which he was appointed first assistant, and then, in 1917 - a teacher. From 1920 to 1924. N. rose from junior member to member of the institute corporation.
In 1917, after the U.S. entry into World War I, N. served as a captain in the U.S. Army Chemical Troops. At this time he discovered the fermentation process, which was used in the production of acetone - a solvent widely used in industrial and scientific purposes.
Returning after the war in the Rockefeller Institute, K. resumed its earlier work on the study of proteins and the study of life expectancy, which led him to the need to clarify the nature of enzymes. In 1902, Mr.. German chemist Eduard Buchner discovered group of proteins. These were the enzymes, or enzymes. They are catalysts that promote the implementation of chemical reactions, such as the process of digestion. When H. begun to explore these vital compounds, their chemical composition was almost unknown. Although many scientists and thought, . that enzymes are protein nature, . famous German chemist Richard Willstatter unsuccessfully tried to get their samples in pure form and as a result came to the conclusion, . that the enzymes are not similar to any of the known organic compounds.,
. Disagreeing with the conclusion Willstatter, Loeb suggested that the enzymes have a protein nature and can therefore be explained from the laws of chemistry
. At the suggestion of Loeb H. in 1920. attempted to obtain pure pepsin - an enzyme that regulates occurring in the stomach digestive process. However, his attempt was unsuccessful, and the scientist, started with the resumption of the work of Loeb, proved that the life of the organism depends on the temperature: high temperature leads to a reduction of its duration. This discovery confirmed Loeb and his belief that life is determined by chemical processes.
In 1926, a time when H. began working in the laboratory of the Rockefeller Institute in Princeton (New Jersey), James B. Sumner from the Medical College of Cornell University published the results of their research urease - an enzyme involved in the cleavage of urea. (Urea is a waste product that is formed in the body as a result of protein metabolism.) Sumner, reporting that he had succeeded in isolating the enzyme in crystalline form, suggested its protein origin. Discovery Sumner had been attacked by many scientists, but H. are inspired by the resumption of studies of pepsin, which 4 years later culminated in separation of crystals of substance, with properties very similar to pepsin.
In 30-ies. N. and his colleagues, among which the most significant contribution was made by Moses Kunitz, identified trypsin, chymotrypsin, and several other enzymes. Their work, experimentally confirmed the theory Sumner, has initiated an intensive study of enzymes. The next step in their research was made in 1935. counterpart N. the Rockefeller Institute for Wendell M. Stanley, who first obtained crystals of tobacco mosaic virus, nucleoprotein. In 1939, Mr.. N. first to isolate a bacterial virus, and in sleduyushem year - diphtheria antitoxin in crystalline form.
During the Second World War H. worked as a consultant and formally served as a researcher at the Research Committee of National Defense. During this period he created a method of automatic detection of chemical weapons.
"For obtaining pure viral proteins' H. and Stanley in 1946. was awarded the Nobel Prize in Chemistry jointly with Sumner. She presented on behalf of the Royal Swedish Academy of Sciences Arne Tiselius. Turning to the N., Tiselius said: 'You and your associates have turned the crystallization of enzymes and other active proteins in the art, and you're in it - the master'. In his Nobel lecture H. said that the experiments conducted by him and his colleagues - the laureates 'support the conclusion that the source of enzyme activity is in itself a protein molecule, and not caused by nonprotein impurities'.
After receiving the Nobel Prize H. seriously engaged in studying viruses, with particular emphasis on clarifying their nature and research on the linkages between them. From 1949 to 1958. He, Professor, University of California at Berkeley, while he served as professor and biophysics at the university laboratory Donner. In 1961. N. was awarded an honorary professor in the resignation of the Rockefeller Institute, and in 1962 - University of California at Berkeley.
In 1917, Mr.. N. married Louise Walker. They had a son and a daughter. Son-H. became Frederick V. Robbins. Died scientist at his home in Uikeberge (Arizona) 27 May 1987. It is always a lot and be happy to do some sport, and sometimes hunted and went fishing.
Among the numerous awards H. - Charles Frederick Chandler Medal, Columbia University (1937), Honorary Diploma of the U.S. government (1948) and the Alexander Hamilton Medal, Columbia University (1961). The scientist was a member of the U.S. National Academy of Sciences, . American Philosophical Society and the American Academy of Arts and Sciences, . well as a foreign member of the British Society of Chemistry, . Royal Society of Arts and the Helgoland Academy of Natural Scientists 'Leopoldina'.,