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Biographical Memoirs Volume 56 (1987) / Chapter Skim
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Stanford Moore
Pages 354-385

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From page 355...
... The education of Stanford Moore began at the age of four at a progressive school in Winnetka, Illinois. When he was six, his father moved to a teaching position in the Law School at the University of Florida; he later accepted a position with Mercer University in Macon, Georgia, where the boy attendect the local public schools.
From page 356...
... from Vanderbilt in 1935 with the bachelor of arts degree, summa cum laude, anct was a recipient of the Founcler's Mecial as the outstanding student in his class. Surprisingly, the Stanford Moore who tended to react a rather reclusive life in later years and generally avoided nonscienunc social activities was a socialite as an undergraduate.
From page 357...
... development of methods for the gravimetric estimation of the amino acid composition of proteins by utilizing selective precipitants. This approach hacI been given new impetus two years earlier when William H
From page 358...
... Bergmann suggested that Stan join forces with Bill Stein to develop the solubility product approach as a routine method for amino acids. There was no way at the time to realize that a scientific collaboration had been initiated that wouIcI last for the remainder of the lifetimes of these two young scientists, certainly one of the longest anct most fruitfu} collaborations in the history of all science.
From page 359...
... 359 these agents were not used during While Bill Stein remained with Bergmann anal his colleagues to conduct the research in New York, Stan enlisted in 1942 to serve as a technical aide on the National Defense Research Committee of OSRD to coordinate university and industrial efforts on the biological actions of chemical warfare agents. His base was in Washington, but he made frequent trips to Dumbarton Oaks, where the National Defense Research Committee had its offices.
From page 360...
... , who hac! demonstrated that useful separations of amino acids and peptides could be obtained with potato starch as the matrix and various two-phase mixtures of the lower alcohols, such as n-butanol, with aqueous organic acids as the eluant.
From page 361...
... With these developments it became possible to refine the chromatographic procedures themselves. In the methods ultimately described in 1949, three runs were required to determine all the amino acicts in a protein hydrolysate.
From page 362...
... The successfu! development of the ion-exchange methoclology not only allowoct a considerable reduction in the time required for analysis of a protein hydrolysate, but for the first time it permitted reliable analyses of the amino acid content of various physiological fluids: urine, plasma' and protein-free extracts of tissues.
From page 363...
... It should be recognized that when the events recorded here were taking place, little more was known about the fundamental chemical structure of proteins than in Emil Fischer's time. It was only in 194S, when Frederick Sanger and his students began elucidating the primary structures of the polypeptide chains in insulin, that convincing evidence was at hand to demonstrate that proteins have unique amino acid sequences.
From page 364...
... The resulting mixture of pepticles was separated by ion-exchange chromatography on a column of sulfonate(1 polystyrene resin by procedures similar to those user] earlier for the separation of amino acids.
From page 365...
... In a series of investigations in which the progress of the reaction at clifferent pH values was followect by amino acid analysis, they showed that inactivation at pH 5 was the result of carboxymethylation on nitrogen-! of histidine-!
From page 366...
... These included the determination of the amino acid sequence of pancreatic deoxyribonuclease; investigation of the reaction of cyanate ion with proteins; structural studies with pepsin; the mechanism of action and structure of streptococcal proteinase; studies of the sequence and the active site of ribonuclease Ti; the isolation of 2',3'cyclic nucleotide 3'-phosphohydrolase and its inhibitor from brain; studies on ribonuclease inhibitors; and many studies on modifications of pancreatic ribonuclease. In addition there were many investigations by younger associates and colleagues in their laboratory at the Rockefeller University on which the names of Moore or Stein do not appear.
From page 367...
... He spent half the time in Brussels, Belgium, setting up a laboratory devotect to amino acic! analysis, and half the year in Cambridge, Englancl, sharing a laboratory with Frederick Sanger when the work on the amino acid sequence of insulin was proceeding.
From page 368...
... This was done at "A Symposium on Protein Chemistry in Tribute to Stanford Moore" at the Rockefeller University on November 4, 1983, at which former members of the Moore-Stein laboratory presented their latest studies and
From page 369...
... STANFORD MOORE 369 others spoke on the contributions of these two memorable indivicluals. ~ N P R E P A R ~ N G T H ~ S M E M O ~ R we have used the brief autobiographical notes deposited in the Academy files by Stanford Moore.
From page 370...
... 1947-49 Chairman, Panel on Proteins, Committee on Growth, National Research Council 1949-52 Associate Member, The Rockefeller Institute 1952-82 Professor and Member, The Rockefeller University 1950 Francqui Chair, University of Brussels 1950-60 Editorial Board, journal of Biological Chemistry 1953 -57 Secretary, Commission on Proteins, International Union of Pure and Applied Chemistry 1961-64 Chairman, Organizing Committee, Sixth International Congress of Biochemistry, New York (1964) 1968 Visiting Professor, Health Sciences, Vanderbilt Univer sity School of Medicine 1970-71 President, Federation of the American Societies for Ex perimental Biology 1974-82 1982 trustee, Vanuerollt university Died, August 23, New York City SELECTED MEMBERSHIPS American Society of Biological Chemists (Treasurer, 1956-59; President, 1966-67)
From page 371...
... STEIN American Chemical Society Award in Chromatography and Electrophoresis, 1964 Richards Medal, American Chemical Society, 1972 Linderstr0m-Lang Medal, Copenhagen, 1972 Nobel Prize in Chemistry, 1972
From page 372...
... Aromatic sulfonic acids as reagents for amino acids. The preparation of l-serine, I-alanine, I-phenylalanine, and l-leucine from protein hydrolysates.
From page 373...
... Chromatography of amino acids on starch columns. Solvent mixtures for the fractionation of protein hydrolysates.
From page 374...
... Chromatographic determination of the amino acid composition of proteins. Cold Spring Harbor Symp.
From page 375...
... Procedures for the chromatographic determination of amino acids on four percent cross-linked sulfonated polystyrene resins.
From page 376...
... The free amino acids of human blood plasma.
From page 377...
... Chromatography of amino acids on sulfonated polystyrene resins.
From page 378...
... Chromatographic determination of amino acids by the use of automatic recording equipment. In: Methods in
From page 379...
... The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations.
From page 380...
... The sequence of amino acid residues around the sulfhydryl group at the active site of streptococcal proteinase.
From page 381...
... Chem., 243:6167-70. Amino acid analysis: Aqueous dimethyl sulfoxide as solvent for the ninhydrin reaction.
From page 382...
... Bovine pancreatic deoxyribonuclease A Isolation, composition, and amino acid sequences of the tryptic and chymotryptic peptides.
From page 383...
... Explanation of the observation of pancreatic ribonuclease activity at pH 4.5.
From page 384...
... Ernesto Scoffone Lecture, Biochemistry of derivatives of pancreatic ribonuclease.
From page 385...
... Pancreatic ribonucleases. In: The Enzymes, ed.


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