John Howard Northrop

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John Howard Northrop
John Howard Northrop.jpg
Born (1891-07-05)July 5, 1891
Yonkers, New York, U.S.
Died May 27, 1987(1987-05-27) (aged 95)
Wickenburg, Arizona, U.S.
Cause of death Suicide
Nationality United States
Alma mater Columbia University
Known for Studies of enzymes
Awards Nobel Prize in Chemistry (1946)
Daniel Giraud Elliot Medal (1939)
Scientific career
Fields Biochemistry
Institutions University of California, Berkeley
Columbia University
Rockefeller University

John Howard Northrop (July 5, 1891 – May 27, 1987) was an American biochemist who, with James Batcheller Sumner and Wendell Meredith Stanley, won the 1946 Nobel Prize in Chemistry. The award was given for these scientists' isolation, crystallization, and study of enzymes, proteins, and viruses.[1] Northrop was a Professor of Bacteriology and Medical Physics, Emeritus, at University of California, Berkeley.[2]

Biography[edit]

Early years[edit]

Northrop was born in Yonkers, New York to John Isaiah, a zoologist and instructor at Columbia University, and Alice Rich Northrop, a teacher of botany at Hunter College. His father died in a lab explosion two weeks before John H. Northrop was born. The son was educated at Yonkers High School and Columbia University, where he earned his PhD in chemistry in 1915. During World War I, he conducted research for the U.S. Chemical Warfare Service on the production of acetone and ethanol through fermentation. This work led to studying enzymes.

Research[edit]

In 1929, Northrop isolated and crystallized the gastric enzyme pepsin[3] and determined that it was a protein. In 1938 he isolated and crystallized the first bacteriophage (a small virus that attacks bacteria), and determined that it was a nucleoprotein. Northrop also isolated and crystallized pepsinogen (the precursor to pepsin), trypsin, chymotrypsin, and carboxypeptidase.

For his 1939 book, Crystalline Enzymes: The Chemistry of Pepsin, Trypsin, and Bacteriophage, Northrop was awarded the Daniel Giraud Elliot Medal from the National Academy of Sciences.[4] He was elected a Fellow of the American Academy of Arts and Sciences in 1949.[5] Northrop was employed by the Rockefeller Institute for Medical Research in New York City from 1916 until his retirement in 1961. In 1949 he joined the University of California, Berkeley as Professor of Bacteriology, and later, he was appointed Professor of Biophysics.[6]

Personal life[edit]

In 1917, Northrop married Louise Walker (1891-1975), with whom he had two children: John, an oceanographer, and Alice, who married Nobel laureate Frederick C. Robbins. Northrop committed suicide in Wickenburg, Arizona in 1987.[7]

References[edit]

  1. ^ "The Nobel Prize in Chemistry 1946 - Preparing Pure Proteins". Retrieved 2008-12-14. 
  2. ^ http://content.cdlib.org/xtf/view?docId=hb967nb5k3&doc.view=frames&chunk.id=div00041&toc.depth=1&toc.id=
  3. ^ Northrop, J. H. (1929), "Crystalline Pepsin", Science, 69 (1796): 580, Bibcode:1929Sci....69..580N, doi:10.1126/science.69.1796.580, PMID 17758437 
  4. ^ "Daniel Giraud Elliot Medal". National Academy of Sciences. Archived from the original on 29 December 2010. Retrieved 16 February 2011. 
  5. ^ "Book of Members, 1780-2010: Chapter N" (PDF). American Academy of Arts and Sciences. Retrieved 15 April 2011. 
  6. ^ "John H. Northrop - Biographical". Nobel Foundation. Retrieved 29 April 2017. 
  7. ^ See p. 440 of Herriott, R. M. (1994), "John Howard Northrop: July 5, 1891-May 27, 1987", Biographical Memoirs. National Academy of Sciences (U.S.), 63, pp. 423–50 

Further reading[edit]

  • Northrop, J. H. (1939), Crystalline Enzymes, Columbia University Press 
  • Shampo, M A; Kyle, R. A. (2000), "John Northrop--definitive study of enzymes", Mayo Clin. Proc. (published March 2000), 75 (3), p. 254, doi:10.4065/75.3.254, PMID 10725951 
  • van Helvoort, T. (1992), "The controversy between John H. Northrop and Max Delbrück on the formation of bacteriophage: bacterial synthesis or autonomous multiplication?", Annals of Science (published November 1992), 49 (6), pp. 545–75, doi:10.1080/00033799200200451, PMID 11616207 

External links[edit]