Arda Green

Arda Green was born in Prospect, Pennsylvania, daughter of Vennis A. Green and Melva Stevenson Green. Her father taught chemistry, and her sister Metta Clare Green (Loomis) earned a PhD in physics. The Green family moved to California when Arda was a girl.[3][4] Arda Green earned undergraduate degrees in chemistry and philosophy at the University of California at Berkeley in 1921; she continued into graduate study of philosophy, but soon shifted her focus to medicine. She earned a medical degree at Johns Hopkins University in 1927.[1]

She started medical studies at Berkeley, but took a year off to study under protein biochemist Edwin J. Cohn at Harvard University at the encouragement of Herbert M. Evans.[2] She then completed her medical studies at Johns Hopkins University, where she worked on electrolyte conductivity in membranes with Leonor Michaelis[5] and graduated in 1927.[1]

After graduate study, Green worked as a National Research Council fellow in medicine at Harvard University, working in the laboratory of Edwin Cohn and specializing in developing methods for isolating and purifying proteins.[2] In the period from 1930 until 1932, Green conducted research at Woods Hole Oceanographic Institution[6] where she worked with Alfred C. Redfield on respiration in porpoises[7] and a project on hemoglobin in certain fish.[8] She collaborated with Ronald M. Ferry on studies into hemoglobin's pH dependence and would later continue characterizing hemoglobin's solubility and interactions with carbon dioxide and carbon monoxide.[2] During her time at Harvard, she also worked as a research fellow in the lab of Lawrence J. Henderson, spent seven years as a research associate in pediatrics, and tutored biochemical sciences at Radcliffe College.[2]

In 1941, she moved to the Washington University in St. Louis in Missouri, where she worked with Gerty Cori and Carl Cori as an assistant professor of biochemistry.[9] Green isolated pure phosphorylase, a key enzyme in the Cori cycle pathway that breaks down the sugar storage molecule glycogen, playing a critical role in the elucidation of glycogen metabolism.[1] At Washington University she also purified other important metabolic enzymes including aldolase, which breaks down fructose.[1]

In 1945, she was appointed to the faculty at the Cleveland Clinic, working with Irvine Page. It was at Cleveland that she co-discovered and named serotonin, an important organic compound, with Page and Maurice M. Rapport.[10] She also isolated and studied, in collaboration with F. M. Bumpus, molecules important in blood pressure regulation including angiotensinogen (the precursor to angiotensin) and angiotonin (hypertension).[2]

Green's career concluded at Johns Hopkins University; she began studying the chemistry of bioluminescence with William D. McElroy at the McCollum-Pratt Institute there in 1953.[11] She isolated firefly luciferase, discovered the reaction that makes fireflies glow, and began work on bacterial bioluminescence, but was unable to complete it due to illness.[1]

Green received the Garvan-Olin Medal from the American Chemical Society in autumn 1957[12] and it was formally awarded posthumously in April 1958.[2]

Green died in January 1958, from breast cancer, at the age of 58.[1]

• Benjamin F Shearer; Barbara Smith Shearer (1997). Notable women in the physical sciences : a biographical dictionary. Westport, Conn. : Greenwood Press, 1997. ISBN 9780313293030. OCLC 433367323.