James B. Sumner
James B. Sumner | |
|---|---|
| Born | November 19, 1887 |
| Died | August 12, 1955 (aged 67) |
| Nationality | United States |
| Alma mater | Harvard University |
| Known for | First to isolate an enzyme in crystallized form First to show that an enzyme is a protein |
| Awards | Nobel Prize in Chemistry (1946) |
| Scientific career | |
| Fields | Chemistry |
| Institutions | Cornell University |
| Doctoral advisor | Otto Folin |
James Batcheller Sumner (November 19, 1887 – August 12, 1955) was an American chemist. He shared the Nobel Prize in Chemistry in 1946 with John Howard Northrop and Wendell Meredith Stanley.
Biography
Sumner graduated from Harvard University with a bachelor's degree in 1910 where he was acquainted with prominent chemists Roger Adams, Farrington Daniels, Frank C. Whitmore, James Bryant Conant and Charles Loring Jackson. In 1912, he went to study biochemistry in Harvard Medical School and obtained his Ph.D. degree in 1914 with Otto Folin. He then worked as Assistant Professor of Biochemistry at Cornell University in Ithaca,NY.
Research
It was at Cornell where Sumner began his research into isolating enzymes in pure form; a feat which had never been achieved before. The enzyme he worked with was urease. Sumner's work was unsuccessful for many years and many of his colleagues were doubtful, believing that what he was trying to achieve was impossible, but in 1926 he demonstrated that urease could be isolated and crystallized. He was also able to show by chemical tests that his pure urease was a protein.[1] This was the first experimental proof that an enzyme is a protein, a controversial question at the time.
His successful research brought him to full professorship at Cornell in 1929. From 1924 on his laboratory was located on the second floor of the new dairy science building,Stocking Hall,{today home to Food Science} at Cornell where he did his Nobel prize winning research. In 1937 he succeeded in isolating and crystallizing a second enzyme, catalase. By this time, John Howard Northrop of the Rockefeller Institute had obtained other crystalline enzymes by similar methods, starting with pepsin in 1929. It had become clear that Sumner had devised a general crystallization method for enzymes, and also that all enzymes are proteins.
Honors and awards
In 1937, he was given a Guggenheim Fellowship and he spent five months in Sweden working with Professor Theodor Svedberg. Also that year, he was awarded the Scheele Medal in Stockholm.
Both Sumner and Northrop shared the Nobel Prize in 1946 for crystallization of enzymes. Sumner was elected to the National Academy of Science in 1948. In 1949, he was elected a Fellow of the American Academy of Arts and Sciences.[2] Sumner died aged 67 of cancer on August 12, 1955.
Notes
While hunting at age 17, Sumner was accidentally shot by a companion and as a result his left arm had to be amputated just below the elbow. He had been left-handed before the accident, after which he had to learn to do things with his right hand.
References
- ^ The chemical nature of enzymes (Nobel lecture) See p.117: "It gave tests for protein and possessed a very high urease activity."
- ^ "Book of Members, 1780-2010: Chapter S" (PDF). American Academy of Arts and Sciences. Retrieved 14 April 2011.
- Sumner's Nobel Foundation biography
- Alexander L. Dounce (1955). "Prof. James B. Sumner". Redox Report. 176 (4488): 859. doi:10.1038/176859a0.
- "Sumner, James B. (1887-1955)". Biographical Memoirs / National Academy of Sciences. 31.
External links
- Sumner's Nobel Lecture The Chemical Nature of Enzymes
- Sumner's Speech at the Nobel banquet
