SUMNER, JAMES BATCHELLER

(b. Canton, Massachusetts, 19 November 1887; d. Buffalo, New York, 12 August 1955)

biochemistry.

The son of Charles and Elizabeth Rand Sumner, James Sumner grew up in a well-to-do New England family engaged in manufacturing and farming. As a boy, he was an enthusiastic hunter, and in consequence of a shooting accident lost the use of his left arm–a misfortune all the more serious because he had been left-handed. With perseverance and ingenuity, he trained himself to use his right hand not only in normal activities but also in sports; he became an expert tennis player and continued to play into his sixties. In 1915 Sumner married Bertha Louise Ricketts; they had five children. After their divorce in 1930, he married Agnes Pauline Lundquist the following year. His second marriage also ended in divorce, and in 1943 Sumner married Mary Morrison Beyer; they had two children.

Upon completing his schooling at the Eliot Grammar School and the Roxbury Latin School, Sumner entered Harvard College in 1906 to study electrical engineering, but shifted to chemistry before graduating in 1910. He then worked briefly in his uncle’s textile plant and taught chemistry at Mount Allison University, Sackville, New Brunswick, and at the Worcester Polytechnic Institute in Massachusetts. He returned to Harvard in 1911 to pursue graduate studies. He received the A.M. degree in 1913 and the Ph.D. degree in biological chemistry in 1914; his dissertation, “The formation of Urea in the Animal Body,” was based on research he conducted under the supervision of O. Folin and in association with C. H. Fiske.

In 1914 Sumner became assistant professor of biochemistry at the Ithaca division of the Cornell University Medical College, and in 1929 he was promoted to full professor. After the division was discontinued in 1938, he was successively a member of the department of zoology and of the department of biochemistry and nutrition in the Cornell School of Agriculture. In 1947 a laboratory of enzyme chemistry was established in the latter department, with Sumner as its director.

Sumner decided, in 1917, to isolate an enzyme; his earlier interest in urea metabolism led him to select urease, which catalyzes the cleavage of urea to ammonia and carbon dioxide. He found this enzyme to be present in relatively large amounts in the jack bean (Canavalia ensiformis); because of his conviction that enzymes are proteins, he concentrated on the fractionation of the proteins of this material. After nine years of effort he succeeded in obtaining a crystalline globulin with high urease activity. He published this result in 1926, a time at which Willstätter was advocating the view that enzymes were low-molecular-weight substances readily adsorbed upon such carrier colloids as proteins. Because of Willstätter’s eminence in chemistry (he had won the Nobel Prize in 1915 for his work on chlorophyll), Sumner’s claim that urease is a protein was not generally accepted by the scientific community. Although he published a series of papers during the years 1926–1930 providing additional data in support of his position, it was not until J. H. Northrop announced, in 1930, the isolation of pepsin in the form of a crystalline protein that the merit of Sumner’s work began to be recognized.

By 1937 several other enzymes had been obtained in crystalline form, and convincing data had been offered for the view that the catalytic activity of enzymes is associated with the integrity of individual proteins. Furthermore, W. M. Stanley had isolated, from plants infected with tobacco mosaic, a crystalline protein (later shown by F.C. Bawden and N. W. Pirie to be a nucleoprotein) that carried the infectivity of the virus. The recognition of Sumner’s achievement was underlined in 1946 by the decision of the Nobel Committee in chemistry to award him one-half of the prize for that year for “his discovery that enzymes can be crystallized,” the other half being shared by Northrop and Stanley.

Because the Willstätter group emphasized the importance of low-molecular-weight substances as bearers of the catalytic activity of enzymes, the iron-porphyrin-containing enzymes peroxidase and catalase were considered around 1930 to represent examples of the adsorption of such small catalytic substances to protein carriers. In 1937 Sumner (with his student A. L. Dounce) reported the crystallization of catalase, and he later provided data to demonstrate its protein nature. During the succeeding years, he published valuable reports on peroxidases, lipoxidase, and other enzymes.

Sumner’s scientific career exemplifies the persistence of the investigator who stubbornly treads a path that his more influential contemporaries consider to be a blind alley. As matters turned out, it was they who were going in the wrong direction, and it was Sumner who had chosen the road that led to the great achievements in enzyme chemistry after 1930.

BIBLIOGRAPHY

I. Original Works. Sumner’s books include Textbook of Biological Chemistry (New York, 1927); Chemistry and Methods of Enzymes (New York, 1943; 2nd ed., 1947; 3rd ed., 1953), written with G. Fred Somers; and Laboratory Experiments in Biological Chemistry (New York, 1944; 2nd ed., 1949), also written with Somers. With Karl Myrbäck, Sumner edited the treatise The Enzymes, Chemistry and Mechanism of Action, 2 vols. (New York, 1950–1952). Sumner published about 125 research articles; among the most important are “The Isolation and Crystallization of the Enzyme Urease (Preliminary Paper),” in Journal of Biological Chemistry, 69 (1926), 435–441; and “Crystalline Catalase,” ibid., 121 (1937), 417–424, written with Alexander L. Dounce.

II. Secondary Literature. An appreciation of Sumner’s life and work is L. A. Maynard’s article in Biographical Memoirs. National Academy of sciences, 31 (1958), 376–396, with portrait and bibliography.

Joseph S. Fruton