Academic journal article Proceedings of the American Philosophical Society

Joseph S. Fruton

Academic journal article Proceedings of the American Philosophical Society

Joseph S. Fruton

Article excerpt

14 MAY 1912 * 29 JULY 2007

JOSEPH S. FRUTON died on 29 July 2007 in New Haven, Connecticut. He was Eugene Higgins Professor Emeritus of Biochemistry and professor emeritus of the history of medicine at Yale University. He had been at Yale, where he led the conversion of the historic Department of Physiological Chemistry into a modern Department of Biochemistry in the Yale graduate school and school of medicine, since 1945. A gifted teacher in the lecture hall, he co-authored with his wife, Sofia Simmonds, General Biochemistry, the first comprehensive and rigorous textbook of biochemistry (Fruton and Simmonds, 1953, 1958). The book was translated into Japanese and various European languages. Several generations of biochemists in many countries were educated using this book, including many who steered the development of molecular biology by merging biochemistry with genetics. Fruton's primary research interests throughout his life were the specificity and mechanism of proteolytic enzymes. His historical research into the history of biochemistry was as distinguished as his laboratory work.

Like many others in his generation, Fruton credited Sinclair Lewis's Arrowsmith as his inspiration for becoming a scientist. As an undergraduate at Columbia College he majored in chemistry. When he graduated from Columbia in 1931, he was already accepted as a graduate student by Hans Thacher Clarke, who was chair of the Columbia Department of Biological Chemistry. The laboratory community provided his first truly sympathetic environment, and several of his colleagues there became his lifelong friends. His thesis research under Clarke concerned the chemical reactivity of cystine derivatives, and he received the Ph.D. degree in 1934.

With Clarke's support, Fruton was appointed as research assistant to Max Bergmann at the Rockefeller Institute for Medical Research (now Rockefeller University). Bergmann, a distinguished and accomplished peptide chemist, had recently arrived in the U.S. in one of the earliest waves of fine German scientists escaping from the Nazi regime. Leónidas Zervas, the gifted Greek peptide chemist, had joined Bergmann for a two-year stay. Earlier, Bergmann and Zervas had collaborated on the development of the seminal carbobenzoxy method for peptide synthesis and studied the dipeptidase of intestinal mucosa. Fruton was asked to continue this work, with special attention to the stereospecificity of the dipeptidase, a matter of great interest to Bergmann. Under the tutelage of Zervas, Fruton succeeded well with the demanding chemical syntheses of various peptides. However, he became frustrated with the impure and uncharacterized enzyme preparations, a concern that was apparently not shared by Bergmann, who had Fruton and others embark on a series of studies of the specificity of papain. The key discoveries for Fruton during this time were Heinz Fraenkel-Conrat's demonstration that papain could catalyze the formation of a peptide bond and confirmation of this with chymotrypsin. Fruton later called these reactions "transamidation" or "transpeptidation." Fruton thought that Bergmann overinterpreted these findings as a path to investigating protein synthesis; he wrote in his memoir that "Bergmann's biological aspirations outstripped the chemical evidence." Although Fruton was very much interested in this work, Bergmann turned the topic over to another researcher. This was a common practice in Bergmann's laboratory and one that added to Fruton's growing frustrations. Later, Fruton would return to transpeptidation.

The crystallization of urease and pepsin by James Sumner in 1926 and John Northrop in 1930, respectively, resolved disputes over whether enzymes are protein molecules, but the basic primary structure of proteins remained controversial. Fruton recognized two important issues concerning this dispute. First, that the analytical methods being used were insufficiently sensitive or quantitative to resolve fundamental questions about protein structure. …

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