William Cumming Rose

William Cumming Rose was born on April 4, 1885 in Greenville, South Carolina. His father, John M. Rose was a Presbyterian minister and the family moved often. Rose attended a variety of local schools until he was 14 when his father removed him from school because it was not providing enough intellectual stimulation. Thereafter he was tutored by his father who introduced him to Greek, Latin, and Hebrew. He a acquired an interest in chemistry from reading Ira Remsen's An Introduction to the Study Chemistry, a textbook used by his sister. Rose wished to attend a large university, but his father, worried for his sixteen year old son, convinced him to attend Davidson College in North Carolina.

At 19 Rose obtained his B.S. degree and went to Yale University and the Sheffield Scientific School. There he studied biochemistry and worked as an assistant in the laboratory of Layfayette Mendel. In Mendel's lab he did a project on creatine/creatinine metabolism, which formed the basis of his doctoral thesis. He graduated in 1911.

After graduating he obtained a position as an instructor in physiological chemistry at the University of Pennsylvania. Then after a short time studying in Germany, in the laboratory of Professor Franz Knoop at the University of Freiburg, he accepted an appointment at the University of Texas, where he organized the first biochemistry course for medical students. He remained in Texas for nine years. In 1922 he went to the University of Illinois, as professor of physiological chemistry (the title was changed to professor of biochemistry in 1936). Rose remained at the University of Illinois until his retirement in 1955.

Although he was interested in many aspects of metabolism, Rose's work focused on amino acid metabolism and nutrition. Amino acids are the units which form proteins (For a review of amino acids see here). There are twenty different amino acids which animals and plants use to put together proteins. Some of these can be synthesized in vivo and a are called nonessential. Others that cannot be synthesized and must come from diet are called essential. In an experiment Rose fed rats with the nineteen amino acids known at the time as their sole source of nitrogen and the rats lost weight. Using the laborious isolation techniques available before chromatography, Rose and his colleagues where able to isolate the amino acid threonine, which when added to the rat's diet allowed them to gain weight.

Over the next twenty years Rose experimented to determine which amino acids were essential and nonessential for rats by excluding them from their diet. He determined that rats required nine essential amino acids (including threonine) in their diet and one, arginine, was only essential for optimal growth. In 1942 Rose began a similar set of experiments to determine which amino acids were essential for humans, using male graduate students as experimental subjects (an account of the experiment can be found here). The subjects urine and feces were examined to determine nitrogen balance. The experiments concluded that there were eight essential required in the human diet.

Rose served on the Food and Nutrition Board of the National Research Council and was instrumental on advising government agencies on nutritional requirements. From 1939 to 1941 Rose served as the president of the American Society of Biochemists. On his ninetieth birthday the William C. Rose Lectureship was established to honor biochemists for outstanding research into biochemistry and molecular biology and a commitment to training younger scientists. The William C. Rose award, as it was renamed, is given annually by the American Society for Biochemistry and Molecular Biology.

Rose died on September 15, 1985.

References:

Carter, Herbert E. and Coon, Minor J.; "William Cumming Rose" at National Academy Press (www.nap.edu)

Roe, Daphne; "William Cumming Rose"; Journal of Nutrition (1981)111:1311-1320

Simoni, Robert D., Hill, Robert L., and Vaughan, Martha; "The Discovery of the Amino Acid Threonine: the Work of William C. Rose"; Journal of Biological Chemistry (2002) 277, e25