Henry Arnold Lardy, past president of the American Society for Biochemistry and Molecular Biology, died Aug. 4, 2010, from prostate cancer, a few days before his 93rd birthday.
Henry Arnold Lardy, one of our most respected biochemists and past president of the American Society for Biochemistry and Molecular Biology, was born Aug. 19, 1917. He died Aug. 4, 2010, from prostate cancer, a few days before his 93rd birthday. He was raised on a farm near Roslyn, S.D. After graduating from high school, Henry received permission from his father to attend one semester at South Dakota State University. Henry found acquisition of knowledge to be addictive and spent the rest of his life in its pursuit. In the fall of 1939, Henry and I started graduate studies at the University of Wisconsin-Madison. This launched our rewarding, lifelong friendship.
Henry’s outstanding qualifications already were evident. After receiving his doctoral degree in l943 and completing a year of postdoctoral study, he was recruited to the faculty of the Wisconsin biochemistry department. He later had a key role in the establishment of the well-recognized Enzyme Institute, and in 1966, he became a prestigious Vilas professor. Although he reached emeritus status in 1988, he continued his research until he was incapacitated by cancer this summer.
Known to associates as Hank, he mentored more than 60 graduate students and 100 postdoctoral fellows over the years. He had an unselfish interest in their training and welfare and deservedly gained their respect and affection. It is likely that more of his past colleagues regard him as one of their best friends than anyone else I know.
His group contributed importantly to a wide swath of enzymology and metabolism, in part because he wanted his students and associates to have their own problems and challenges. In 2005, the leading journal in his field – the Journal of Biological Chemistry – celebrated its centenary by reprinting a series of classics (1). They chose three of the approximately 150 papers Henry published in the JBC.
One of these papers reported the important finding that respiratory rate could be controlled by the availability of acceptors for a phosphate group from the ATP formed by respiration. This finding provided the basis for the measurement of oxygen uptake as a probe of respiratory control; 2,4-dinitrophenol stimulated oxygen uptake by uncoupling electron transport from ATP formation. Another of Henry’s JBC papers included the first demonstration that the formation of phosphopyruvate from ATP and pyruvate was metabolically reversible.
The third paper provided an explanation of an old problem: how glyceraldehyde inhibits glycolysis. The paper noted that the L-glyceraldehyde, but not the D form, was inhibitory. It also traced the inhibition to the L-sorbose 1-phosphate formed. This finding was explained by the structural similarity of the L-sorbose 1-phosphate and the glucose 6-phosphate, a product of the hexokinase reaction.