Stanford Moore was an American biochemist who shared the 1972 Nobel Prize in Chemistry with two other American biochemists, William Howard Stein and Christian B. Anfinsen, for his work at ‘Rockefeller University’ on the structure of ribonuclease, a type of nuclease, and also for understanding the relationship between the chemical structure of the ribonuclease molecule and its catalytic activity. Moore and Stein collaborated to develop novel chromatographic techniques for analyzing amino acids and small peptides obtained through protein hydrolysis. The duo developed the first automatic amino-acid analyzer, which greatly facilitated the study of protein amino acid sequences. They used the new device to conduct the first analysis of the complete chemical structure of the enzyme ribonuclease. Moore spent the majority of his professional career at ‘Rockefeller University,’ with the exception of a brief stint with the United States government during the ‘Second World War.’ In 1954, he was awarded a ‘Doctor honoris causa’ by the Faculty of Medicine of the ‘University of Brussels. Along with fellow biochemist William H. Stein, he received several awards, including the American Chemical Society Award in Chromatography and Electrophoresis in 1964, the Carlsberg Research Center’s ‘Linderstrom-Lang Medal’ in 1972, and the American Chemical Society’s ‘Richards Medal’ in 1972.
Childhood & Adolescence
He was born in Chicago, Illinois, on September 4, 1913, to John Howard Moore and his wife Ruth Moore. He was raised in Nashville, Tennessee, where his father taught at Vanderbilt University’s ‘Vanderbilt University Law School.’
He attended the ‘Peabody Demonstration School’ (now known as the ‘University School of Nashville’), a Nashville high school run by the ‘George Peabody College for Teachers’.
He then enrolled at Vanderbilt University, where he graduated summa cum laude (meaning “with the highest honor”) in 1935 with a major in chemistry.
He was a member of the university’s Phi Kappa Sigma fraternity. The faculty recommended that he apply for a Wisconsin Alumni Research Foundation Fellowship, and he enrolled at the ‘University of Wisconsin’ for postgraduate doctoral studies.
He received a doctorate in organic chemistry from the ‘University of Wisconsin’ in 1938. He completed his thesis in biochemistry in the laboratory of American biochemist Karl Paul Gerhard Link.
He acquired the microanalytical procedures for analyzing C, H, and N developed by Slovenian-Austrian chemist and physician Fritz Pregl from Link. This lesson imparted by Link proved to be extremely beneficial for him in his subsequent scientific works involving quantitative protein analysis.
Career of Stanford
He joined Max Bergmann’s laboratory at the ‘Rockefeller Institute for Medical Research’ in New York in 1939, a friend of Link’s. This internationally renowned institute was renowned for its research on the chemistry of enzymes and proteins.
His research with a group of gifted chemists in Bergmann’s lab was interrupted after three years in 1942, when he was enlisted as a technical assistant in the ‘National Defense Research Council’ in Washington during the ‘Second World War’. He served in that capacity until 1945.
He worked on academic and industrial chemical projects for the ‘Office of Scientific Research Development’ and later for the ‘Operational Research Section’ at the US armed forces’ headquarters in Hawaii.
He returned to the Rockefeller Institute following the war, accepting an offer from then-Director Herbert Gasser, who gave him and William H. Stein the freedom and space to conduct research in their field of interest.
He applied and also invented new methods for determining the peptides and amino acids found in biological fluids and proteins. He developed a photometric ninhydrin procedure for use in amino acid chromatography.
Moore and Stein succeeded in isolating individual amino acids from a synthetic mixture; their work was published in the peer-reviewed scientific journal ‘Journal of Biological Chemistry’. The pair used their methods to determine the structures of bovine serum albumin and -lactoglobulin.
From 1947 to 1949, he chaired the Panel on Proteins of the National Research Council’s Committee on Growth.
He remained a Francqui Chair scholar at the ‘University of Brussels’ until 1950.
Between 1950 and 1951, he was a chemistry scholar at the ‘University of Cambridge’ and then a biochemistry scholar for a year at the ‘Rockefeller Institute for Medical Research’.
From 1950 to 1960, he served on the Editorial Board of the ‘Journal of Biological Chemistry.’
In 1952, he was appointed Professor of Biochemistry at the ‘Rockefeller Institute for Medical Research,’ a position he held until 1965.
He served as Secretary of the International Union of Pure and Applied Chemistry’s Commission on Proteins from 1953 to 1957.
He was elected Treasurer of the ‘American Society for Biochemistry and Molecular Biology’ in 1956, a position he held until 1959. He served as President of the society in 1966.
In 1958, he and Stein developed the first automatic amino-acid analyzer, which greatly facilitated the analysis of protein amino acid sequences and also enabled the composition of the enzyme ribonuclease to be determined.
In 1959, the duo published the first analysis of ribonuclease’s complete amino acid sequence. Additionally, the two biochemists investigated the structure, function, and association of several other proteins, including pancreatic ribonuclease, ribonuclease T1, pepsin, chymotrypsin, pancreatic deoxyribonuclease, and streptococcal proteinase.
Moore was appointed Chairman of the International Congress of Biochemistry’s Organizing Committee in 1964.
He was a Professor of Biochemistry at the ‘Rockefeller University’ from 1965 to 1982.
In 1968, he served as a Visiting Professor of Health Sciences at Vanderbilt University School of Medicine.
He served as President of the ‘Federation of American Societies for Experimental Biology’ in 1970.
He was a fellow of the ‘American Academy of Arts and Sciences,’ the ‘National Academy of Sciences,’ and the ‘Harvey Society,’ as well as a foreign member of the ‘Belgian Biochemical Society’ and the ‘Belgian Royal Academy of Medicine.
Personal History and Legacies
Moore remained unmarried for the remainder of his life. He was a victim of the always fatal neurological disease amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig’s disease, which attacks the neurons that control voluntary muscles, resulting in muscle degeneration.
This resulted in his gradual immobility, which forced him to spend the majority of his later years at home. On August 23, 1982, in New York City, he succumbed to the disease.
Moore bequeathed his property to ‘Rockefeller University’ with the instruction that it be used “as an endowment for the salary or research expenses, or both, of an investigator in the field of biochemistry.”
Estimated Net Worth
Stanford Moore’s net worth or earnings are estimated to be between $1 million and $3 million. He amassed such wealth through his primary career as a chemist.
Trivia
He served on a federal grand jury investigating the Cosa Nostra, a criminal syndicate, in the early 1960s.