Stanford Moore was an American biochemist who was jointly awarded the ‘Nobel Prize in Chemistry’ in 1972
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Stanford Moore was an American biochemist who was jointly awarded the ‘Nobel Prize in Chemistry’ in 1972
Stanford Moore born at
Moore remained unmarried throughout his life.
He was a victim of the invariably fatal neurological disease amyotrophic lateral sclerosis (ALS), commonly called the Lou Gehrig's disease that attack the neurons which control the voluntary muscles thus causing muscle degeneration. This resulted in his gradual immovability that left him mostly in-house during the later stage of his life. He finally succumbed to the disease on August 23, 1982, in New York City.
Moore handed out his property to the ‘Rockefeller University’ with instructions "to be used as endowment toward the salary or research expenses or both of an investigator in the field of biochemistry".
He was born on September 4, 1913, in Chicago, Illinois, to John Howard Moore and his wife Ruth Moore. He was raised in Nashville, Tennessee, where his father was a faculty member of the ‘Vanderbilt University Law School’.
He attended ‘Peabody Demonstration School’ (at present called the ‘University School of Nashville’), a high school in Nashville which was managed by the ‘George Peabody College for Teachers’.
Thereafter he enrolled at the ‘Vanderbilt University’ from where he graduated summa cum laude (meaning: "with highest honor") with chemistry major in 1935. He was a Phi Kappa Sigma member at the university. He was recommended a Wisconsin Alumni Research Foundation Fellowship by the faculty following which he joined the ‘University of Wisconsin’ for his postgraduate doctoral studies.
In 1938 he earned a PhD in organic chemistry from the ‘University of Wisconsin’. He conducted his thesis in biochemistry under the guidance of American biochemist Karl Paul Gerhard Link in the latter’s laboratory.
He learned the microanalytical procedures developed by Slovenian-Austrian chemist and physician Fritz Pregl for analysing C, H, and N from Link. This lesson imparted by Link proved to be extremely valuable for him in his future scientific works related to quantitative analysis of proteins.
In 1939 he joined the laboratory of Max Bergmann, a friend of Link, at the ‘Rockefeller Institute for Medical Research’ in New York. This institute of international repute was renowned for its investigations on the chemistry of enzymes and proteins.
His research work with a group of talented chemists, which included William H. Stein, in the lab of Bergmann, got interrupted after three years in 1942 when he was enlisted as a technical aid in the ‘National Defense Research Council’ in Washington during the ‘Second World war’. He served the position till 1945. He worked in the academic and industrial chemical projects that were managed by the ‘Office of Scientific Research Development’ and later served the ‘Operational Research Section’ linked with the headquarters of the US armed forces in Hawaii.
Post war he returned to the Rockefeller Institute accepting offer of the then Director Herbert Gasser who provided him and William H. Stein with the liberty and space of conducting research work of their line of interest.
He applied and also developed new uses of chromatography to determine the peptides and amino acids present in biological fluids and proteins. He evolved a procedure of photometric ninhydrin for applying in amino acids chromatography.
Moore and Stein became successful in separating out individual amino acids from a synthetic mixture, a work that was featured in the peer-reviewed scientific journal ‘Journal of Biological Chemistry’. The duo applied their procedures to analyse the structures of bovine serum albumin and β-lactoglobulin.
In the early 1960s he served a federal grand jury that was investigating the Cosa Nostra, a criminal syndicate.