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STANFORD MOORE September4, 1913-August23, 1982 BY EMIL L. SMITH AND C. H. W. HIRS ST A N F O R D M O O R E, Nobel Laureate in Chemistry in 1972, was born in Chicago, Illinois, when his father, John Howard Moore, was a student at the. University of Chicago Law School ~ }.D., 19171. His father was a graduate of West- minster College in New Wilmington, Pennsylvania, and his mother knee Ruth Fowler) of Stanford University. His par- ents were married in 1907 and hac! met at Stanford. It is alleged that this was the origin of the given name of the son. 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 posi- tion with Mercer University in Macon, Georgia, where the boy attendect the local public schools. In 1924 I. H. Moore became professor of law at Vanclerbilt University, where he was to serve on the faculty until his retirement in 1949; he liecl in 1966 at the age of eighty-five. In Nashville, Stanford was a student at Peabody Demon- stration School, which was operated by the George Peabody College for Teachers. He was an outstanding student for the seven years he attencled the school, and he maintained a straight A average. Initially his interests were in English and science, and he was fortunate to encounter a teacher, R. O. 355

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356 ~ T ~, . BIOGRAPHICAL MEMOIRS Beauchamp, who arouser! his interest in chemistry. In 1931 he entered the College of Letters and Science of Vanclerbilt university, cons~cter~ng a career in aeronautical engineering or chemistry. Unable to decide between the two fields, he pursued both the liberal arts and the basic subjects of the engineering curriculum during his first two years. In his thirc! year at Vanderbilt, he came under the influence of Ar- thur William Ingersoll, who Stan later creclited as stimulating his enthusiasm for organic chemistry and molecular struc- ture. As a result, Stan changed his major subject to chemistry and graduates! 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. Sur- prisingly, the Stanford Moore who tended to react a rather reclusive life in later years and generally avoided nonscien- unc social activities was a socialite as an undergraduate. He was active in several clubs, president of his fraternity, ancl, as president of the student council, the organizer of the senior A: L: ~ ~ ~ _ 1 ~ prom. In the autumn of 1935, Stan enterer! the Graduate School of The University of Wisconsin with the support of a fellow- ship from the Wisconsin Alumni Research Foundation. Al- though he chose to major in organic chemistry, he elected to do his thesis research with Professor Karl Paul Link, a mem- ber of the Biochemistry Department at Madison. It was sig- nificant for Stan's later development that Link had spent some time years earlier in Graz, Austria, in the laboratory of Fritz Preg1, one of the pioneers in the clevelopment of microanalytical methods. Link required all of his students to master these microanalytical techniques. In retrospect it is apparent that Stan's background, first in engineering and then in microanalysis, hac! an important effect on his later collaborative work with William H. Stein in the development of important new methods of automated analysis.

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STANFORD MOORE 357 Moore's thesis research (ultimately summarized in five pa- pers) included a study of the reaction of o-phenylenediamine with various monosaccharides. The products of this reaction, a series of benzimidazoles, project to be readily isolatec! as stable crystalline solids that lent themselves well to the iden- tification of various monosaccharides. These derivatives con tinue to be so used. With the completion of his doctoral dissertation (1939), it was clear that Stan's future was to be in biochemistry. Two attractive options were available: a four-year fellowship at Harvard Medical School and an invitation to become a re- search assistant in the laboratory of Max Bergmann at the Rockefeller Institute for Medical Research in New York. Bergmann hac! been one of Emil Fischer's outstanding col- laborators, and he hac! continued after the First WorIct War to make a series of notable contributions in protein ant! car- bohyctrate chemistry while at the Kaiser Wilhelm Institut fuer Lederforschung in Dresden. With the rise of the Nazi dicta- torship in the early 1930s, Bergmann accepted an offer to join the staff of the Rockefeller Institute, and moved there in 1934. It was through Link's friendship with Bergmann that the invitation for Stanford to go to Rockefeller was pre- sented. As Stan commented later, "The question of whether it would be wiser to go on to medical school or to enter im- mectiately into chemical research was resolved in favor of the latter." When Stan joined Bergmann's group, he became involved in one of the principal concerns of the laboratory, the struc- tural chemistry of proteins. Of particular interest was the . 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. Stein joined the laboratory ant! showocI that aromatic sulfonic acids possess desirable prop /

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358 BIOGRAPHICAL MEMOIRS erties in that regard. Whereas earlier workers had concen- tratect on precipitants that formed highly insoluble salts with amino acids (the prototype was flavianic acid, user] by A. Kos- se} and R. E. Gross in 1924 for the isolation of arginine), the research in Bergmann's group emphasized the fact that salts of extremely low solubility were unnecessary, provicl~ec! that the precipitant was selective and that the solubility products of the salts were estimated and corrections were applied for the quantity of amino acid remaining in solution. 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 fruit- fu} collaborations in the history of all science. Bill and Stan concentrated their initial efforts on two sul- fonic acid reagents 5-nitronaphthalene-2-sulfonic acid for glycine anct 2-bromotoluene-5-sulfonic acid for leucine and showed that good results could be obtained with hycirolysates of egg albumin and silk fibroin. But with the work well uncler way, the research tract to be terminated when the country suct~enly founc! itself at war at the end of 1941. With the advent of the war, Bergmann's laboratory un- clertook research for the Office of Scientific Research ant] Development (OSRD). Their specific mission was to investi- gate the physiological actions of vesicant war gases Mustard gas, nitrogen mustards) at the molecular level, with the hope of c:leveloping therapeutic agents that might be helpful in overcoming the effects of these compounds on the human body. The rationale for the work was that adequate defensive measures for preventing the ejects of these toxic com- pounds, as well as the retaliatory capabilities of the United States and its allies, would inhibit the use of chemical warfare

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STANFORD MOORE agents. Fortunately, the war. 359 these agents were not used during While Bill Stein remained with Bergmann anal his col- leagues 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 war- fare agents. His base was in Washington, but he made fre- quent trips to Dumbarton Oaks, where the National Defense Research Committee had its offices. Later (1944), Stan was appointed to the Project Coordination Staff of the Chemical Warfare Service, which was clirectecI by William A. Noyes, Jr. The experiences of the service were summarizer] in a volume published after the war, to which Stan (with W. R. Kirner) contributed an article on the physiological mechanisms of action of chemical warfare agents. When the war endecI, Stan was in Hawaii with the Operational Research Section of the Chemical Warfare Service. Max Bergmann died of cancer in 1944 at age fifty-eight. The war work of the laboratory, however, was continuer! by his associates until the encI of hostilities in 1945. At that time most of them moved elsewhere, and the department that Bergmann hacI organizer! was dissolved. At this juncture Herbert Gasser, then director of the Rockefeller Institute, had the wisdom to offer Bill Stein ant! Stan Moore space in the former Bergmann department, along with the opportu- n~ty-on a trial basis to continue the work on amino acid analysis that they had initiates! before the war. In the interim the collaborative efforts of A. I. P. Martin and R. L. M. Synge ant] their associates in EnglancI procluced novel fractionation techniques, notably partition chromatog- raphy. Bill and Stan were aware of this research, although during the war journals arrived from England rather irreg- ularly. When their collaboration was renewoct in 1945, they .

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360 BIOGRAPHICAL MEMOIRS decided to explore the possibilities a~orclect by partition chromatography for determining the amino acid composi- tions of proteins. Their work took place in parallel with that of Lyman C. Craig, whose laboratory was located on the same floor and who had been exploring the potential of counter- current distribution in the fractionation of pepticle antibi- OtiCS. As a starting point, Bill and Stan clecidect to develop a column chromatographic method basecI on work by S. R. Els- den and Synge (1941), who hac! demonstrated that useful separations of amino acids and peptides could be obtained with potato starch as the matrix and various two-phase mix- tures of the lower alcohols, such as n-butanol, with aqueous organic acids as the eluant. To render the procedure quan- titative, a suitable micro method for the determination of amino acids in the column effluent was required. To this anti, Bill and Stan stuctiec] the ninhydrin reaction, known since its discovery in 191 ~ to result in the formation of colorer! procI- ucts from all amino acids. They cliscoverecl that reproclucible yields of the product could be obtained when the reaction was concluctecl in the presence of a reducing agent, initially stannous chIoricle. To monitor the progress of the separations effecteci on the starch columns, the eluate was collected in small fractions of equal volume; these were treater] with ninhydrin under reducing conditions, and the colored products were mea- sured spectrophotometrically. The concentrations of colorer] product in each fraction were plotted against fraction num- ber to obtain a so-called effluent-concentration curve. The area uncler each peak on such curves gave the amount of amino acid in the sample. Initially the fractions were collected manually, but the la- bor involved quickly lect to the design and construction of an instrument in which each drop of effluent from a column was

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STANFORD MOORE 361 macle to interrupt a light beam incident on a photocell, thereby incrementing a counter. Drops were collectecI into spectrophotometer tubes. When a precleterminect number of drops tract been collectect, a turntable aclvanced to bring a new tube into line. Although this instrument was not the first fraction collector to be describect, it became the prototype for the commercial instruments that soon appearance thereafter in laboratories around the world. With these developments it became possible to refine the chromatographic procedures themselves. In the methods ul- timately described in 1949, three runs were required to de- termine all the amino acicts in a protein hydrolysate. Bill and Stan clescribec! the application of the method to the deter- mination of the compositions of beta-lactogIobulin and serum albumin. The three runs requires! a total of less than 5 milligrams of protein, with a standard error of less than 5 percent, a remarkable achievement at the time. Recognizing the impact this methodology wouIcl have in biochemistry, Bill anti Stan went to considerable lengths to provide cletailecl descriptions of all the necessary steps for the successful ap- plication of their procedures in other laboratories. Most of this information was circulatecI in the form of preprints, well in advance of publication, to anyone desiring access to it. They were to repeat this service to the biochemical commu- nity many times in subsequent years as improvements in methodology were made. In 1949 Herbert Gasser decided that Moore and Stein had demonstrated the competence as indepenclent investi- gators that he hac! hoper! they wouIct develop. As a result the research budget for their laboratory was increased substan- tially. This permitted the recruitment of postdoctoral asso- ciates and additional technical assistants over the next several years, increasing the scope of the research. Space limitations preclude mention of the numerous students and postcloc

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362 BIOGRAPHICAL MEMOIRS toral associates who from this time onward were affiliatecI with the Moore and Stein laboratory. The interested reacler is referred to the bibliography of this memoir for further . ~ . Information. Although the starch column procedures represented a breakthrough of the utmost significance in protein chemistry, there were some limitations. First, there was the slow flow rare of the columns (one complete analysis of a protein hy- drolysate required two weeks). Moreover, a fresh column hacI to be prepared for each run, and the separations were sen- sitive to the presence of salts in the sample. Bill and Stan therefore decided to investigate ion-exchange chromatogra ~. ~r phy on sulfonated polystyrene resins as an alternative. They were encourages] by the success attainer! by S. Miles Partridge in England in the preparative-scale fractionation of amino acids by displacement chromatography on such resins. Effective separations of all the amino acids in a protein hydrolysate in a single run were quickly obtained by elusion with sodium citrate and acetate buffers of increasing pH and concentration at various temperatures, but a great deal of painstaking effort was required to stanciarclize the perform- ance of the columns. The problems were finally overcome when more reproclucible resins became available. The suc- cessfu! 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 var- ious physiological fluids: urine, plasma' and protein-free ex- tracts of tissues. These methods also resulted! in the discovery and estimation of new components of these fluids. Concurrently, the potential of ion-exchange chromatog- raphy for the separation of peptizes ant! proteins was clevel- oped. It was soon found that certain stable, basic proteins- notably bovine pancreatic ribonuclease and chymotrypsino

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STANFORD MOORE 363 yen, and egg-white lysozyme could be chromatographed effectively on TRC-50, a polymethacrylic acid resin. The elu- tion of these proteins from the exchanger occurred in a pre- dictable way in response to changes in pH and ionic strength. Somewhat later the successful fractionation of histories from calf thymus was achieved. Encouraged by these successes, in 1953 Bill and Stan felt the time had arrived to embark on the structural analysis of a protein. It should be recognized that when the events re- corded 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. Sanger's success with the insulin chains (21 and 30 residues) showed that the structure of a polypeptide could be deduced from the sequences of smaller peptides derived from it by selective, partial hydrolysis with weak acid or enzymes. Sanger's work also emphasized the problems of separating the complex mixtures of peptides that resulted from such hydrolysis. It was clear, however, that the deter- mination of the primary structure of longer polypeptide chains would be difficult, if not impossible, by the methods used with the relatively small polypeptide chains of insulin. With this background the choice of a protein became a critical decision for Moore and Stein. They elected to inves- tigate the small enzyme ribonuclease, which they had already studied, arguing that knowledge of its structure would almost certainly aid in understanding its enzymic activity. Their work was performed in parallel with that of Christian B. An- finsen and his colleagues in Bethesda, but the approaches of the two laboratories were different and they functioned on a collaborative rather than competitive basis. Indeed, neither

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364 BIOGRAPHICAL MEMOIRS Bill nor Stan relished competition in science, although they recognizes! its value in expediting progress. The investigation of the structure of ribonuclease starter! with a sample of the oxidized protein that was hyclrolyzed selectively with the proteolytic enzyme trypsin. The resulting mixture of pepticles was separated by ion-exchange chro- matography on a column of sulfonate(1 polystyrene resin by procedures similar to those user] earlier for the separation of amino acids. The compositions of these peptides showed that the entire sequence (124 residues of ribonuclease was rep- resented. To establish how these pepticles originated, the ox- i(lizec! enzyme was next hydrolyzed with chymotrypsin, a protease with a selectivity different from that of trypsin, to produce a second set of peptides that were likewise separates] on sulfonated polystyrene. From the known selectivities of trypsin and chymotrypsin, largely elucidated years earlier by Bergmann and his colleagues, the order of the trYntic nen- tides in the polypepticle chain was clecluced. Confirmation was obtainer! from another set of pepticles isolated from a peptic hydrolysate. As this work proceeded, it was evident that progress was limited by the rate at which amino acict analyses couIct be performed. With the manual methods then in use, a single run required almost three days and several hundrec! spectro- photometer readings. Thus, work was initiated in 1956 to clevelop automated amino acid analysis. It was only after ex- tensive refinement of the instrumentation that the method was published in 195X. With the resins then available, the analysis time was shortened to twenty-four hours ant! the sensitivity permitted runs on as little as 0.5 micromole. Sub- sequent clevelopments have resultecI in a reduction for the time of analysis to an average of about an hour and increased sensitivity by two orclers of magnitude. The benefits to our , 1 1 1

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STANFORD MOORE 375 With }. P. Dustin, C. Czajkowska, and E. I. Bigwood. A study of the chromatographic determination of amino acids in the presence of large amounts of carbohydrate. Anal. Chim. Acta, 9:256- 62. With I. Close, E. L. Adriacns, and E. i. Bigwood. Composition en acides amines d'hydrolysats de farine de maniac Roui variete amere. Bull. Soc. Chim. Biol., 35:985-92. With }. P. Dustin, E. Schram, and E. i. Bigwood. Dosage chroma- tographique des acides amines d'une graine de cereale forget, d'un fain, et d'un tourteau de tin. Bull. Soc. Chim. Biol., 35:1137-49. With C. H. W. Hirs and W. H. Stein. A chromatographic investi- gation of pancreatic ribonuclease. }. Biol. Chem., 200:493-506. With }. Close, and E. i. Bigwood. Amino acid composition of a preparation of crystallized papain. Enzymologia, 16: 137 - 42. 1954 With P. Soupart and E. J. Bigwood. Amino acid composition of human milk. I. Biol. Chem., 206:699-704. With E. Schram and E. }. Bigwood. Chromatographic determina- tion of cystine as cysteic acid. Biochem. }., 57:33-37. With A. Dreze and E. }. Bigwood. On the desalting of solutions of amino acids by ion exchange. Anal. Chim. Acta., 11:554-58. With H. H. Tallan and W. H. Stein.3-Methylhistidine, a new amino acid from human urine. i. Biol. Chem., 206:825-34. With A. G. Bearn and W. H. Stein. The amino acid content of the blood and urine in Wilson's disease. I. Clin. Invest., 33:410-19. With A. C. Paladini, C. H. W. Hirs, and W. H. Stein. Phenylacetyl- glutamine as a constituent of normal human urine. I. Am. Chem. Soc., 76:2848. With C. H. W. Hirs and W. H. Stein. The chromatography of amino acids on ion exchange resins. Use of volatile acids for elusion. I. Am. Chem. Soc., 76:6063-65. With W. H. Stein. Procedures for the chromatographic determi- nation of amino acids on four percent cross-linked sulfonated polystyrene resins. I. Biol. Chem., 211:893-906. With W. H. Stein. A modified ninhydrin reagent for the photo- metric determination of amino acids and related compounds. }. Biol. Chem., 211:907-13.

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376 BIOGRAPHICAL MEMOIRS With W. H. Stein. The free amino acids of human blood plasma. l. Biol. Chem., 211:915-26. With H. H. Tallan and W. H. Stein. Studies on the free amino acids and related compounds in the tissues of the cat. i. Biol. Chem., 211 :927-39. With C. H. W. Hirs and W. H. Stein. The amino acid composition of ribonuclease. I. Biol. Chem., 211:941-50. 1955 With C. F. Crampton and W. H. Stein. Chromatographic fraction- ation of calf thymus histone. I. Biol. Chem., 215: 787-901. With H. H. Tallan, S. T. Bella, and W. H. Stein. Tyrosine-O-sulfate as a constituent of normal human urine. i. Biol. Chem. 217:703-8. With C. H. W. Hirs and W. H. Stein. Studies on the structure of ribonuclease. Proc. 3rd Int. Congr. Biochem., p. 11. Brussels. With i. P. Dustin and E. }. Bigwood. Chromatographic studies on the excretion of amino acids in early infancy. Metabolism,4:75- 79. 1956 With H. H. Tallan and W. H. Stein. N-Acetyl-l-aspartic acid in brain. }. Biol. Chem., 219:257-64. With C. H. W. Hirs and W. H. Stein. Peptides obtained by tryptic digestion of performic acid-oxidized ribonuclease. }. Biol. Chem., 219:623-42. With I. L. Bailey and W. H. Stein. Pentides obtained by peptic hy- drolysis of performic Chem., 221: 143-50. ~ 1 acid-oxidized ribonuclease. I. Biol. With C. H. W. Hirs and W. H. Stein. Peptides obtained by chymo- tryptic hydrolysis of performic acid-oxidized ribonuclease. A partial structural formula for the oxidized protein. I. Biol. Chem., 221:151-69. With W. H. Stein and C. H. W. Hirs. Studies on structure of ribo- nuclease. Fed. Proc. Fed. Am. Soc. Exp. Biol., 15:840-48. With W. H. Stein. Column chromatography of peptides and pro- teins. Adv. Protein Chem., 11: 191-230.

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STANFORD MOORE 1957 377 With C. F. Crampton and W. H. Stein. Comparative studies on chromatographically purified histones. }. Biol. Chem., 225:363-86. With H. G. Kunkel, R. D. Cole, D. H. Spackman, and W. H. Stein. Observations on the amino acid composition of human hemo- globins. Biochim. Biophys. Acta, 24:640-42. 1958 With W. H. Stein. Determination of the structure of proteins: Stud- ies on ribonuclease. Harvey Lect., 1956 -57: 119 - 43. With C. H. W. Hirs and W. H. Stein. Studies on the structure of ribonuclease. In: Symposium on Protein Structure, ed. A. Neuber- ger, pp. 211-22. London: Methuen; New York: John Wiley & Sons. With H. H. Tallan and W. H. Stein. L-cystathionine in human brain. }. Biol. Chem., 230:707-16. With W. H. Stein and D. H. Spackman. Chromatography of amino acids on sulfonated polystyrene resins. Anal. Chem., 30:1185- 90. With D. H. Spackman and W. H. Stein. Automatic recording ap- paratus for use in the chromatography of amino acids. Anal. Chem., 30: 1190 -206. With W. H. Stein and D. H. Spackman. Automatic recording ap- paratus for use in the chromatography of amino acids. Fed. Proc. Fed. Am. Soc. Exp. Biol., 17:1107-15. With R. D. Cole and W. H. Stein. On the cysteine content of human hemoglobin. i. Biol. Chem., 233:1359-63. 1959 With H. G. Gundlach and W. H. Stein. The nature of the amino acid residues involved in the inactivation of ribonuclease by io- doacetate. I. Biol. Chem., 234:1754-60. With H. G. Gundlach and W. H. Stein. The reaction of iodoacetate with methionine. }. Biol. Chem., 234: 1761-64. On the constitution of histones. Onzieme Conseil de Chimie, Inst. Int. de Chimie Solvay, Les Nucleoproteins, pp. 77-103. Bruxelles: Editions Stoops; New York: Interscience.

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378 BIOGRAPHICAL MEMOIRS 1960 With C. H. W. Hirs and W. H. Stein. The sequence of the amino acid residues in performic acid-oxidized ribonuclease. I. Biol. Chem., 235:633-47. With D. H. Spackman and W. H. Stein (with the assistance of Anna M. Zamoyska). The disulfide bonds of ribonuclease. l. Biol. Chem., 235:648-51. With M. P. Brigham and W. H. Stein. The concentrations of cys- teine and cystine in human blood plasma. J. Clin. Invest., 39: 1633-38. With G. R. Stark and W. H. Stein. Reactions of the cyanate present in aqueous urea with amino acids and proteins. I. Biol. Chem., 235:3177-81. With W. H. Stein, R. D. Cole, and G. Gundlach. On the cleavage of disulfide bonds in proteins by reduction. Proc. Fourth Int. Congr. Biochem. 8 Proteins, pp. 52-62. London: Pergamon Press. 1961 With W. H. Stein. The chemical structure of proteins. Sci. Am. 204:S 1-92. With G. R. Stark and W. H. Stein. Relationship between the con- formation of ribonuclease and its reactivity toward iodoacetate. J. Biol. Chem., 236:436-42. 1962 With N. P. Neumann and W. H. Stein. Modification of the methi- onine residues of ribonuclease. Biochemistry, 1:68-75. With D. G. Smyth and W. H. Stein. On the sequence of residues 11 to 18 in bovine pancreatic ribonuclease. I. Biol. Chem., 237: 1845-50. With A. M. Crestfield and W. H. Stein. On the aggregation of bo- vine pancreatic ribonuclease. Arch. Biochem. Biophys., Suppl. 1:217-22. 1963 With W. H. Stein. Chromatographic determination of amino acids by the use of automatic recording equipment. In: Methods in

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STANFORD MOORE 379 Enzymology, ed. S. P. Colowick and N. O. Kaplan, vol.6, pp.819- 31. New York: Academic Press. With D. G. Smyth and W. H. Stein. The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations. I. Biol. Chem., 238:227-33. On the determination of cystine as cysteic acid. i. Biol. Chem., 238:235-37. With T.-Y. Liu, N. P. Neumann, S. D. Elliott, and W. H. Stein. Chemical properties of streptococcal proteinase and its zymo- gen. J. Biol. Chem., 238:251-56. With A. M. Crestfield and W. H. Stein. On the preparation of bo- vine pancreatic ribonuclease A. i. Biol. Chem., 238:618-21. With A. M. Crestfield and W. H. Stein. The preparation and en- zymatic hydrolysis of reduced and S-carboxymethylated pro- teins. J. Biol. Chem., 238:622-27. With G. Jones and W. H. Stein. Properties of chromatographically purified trypsin inhibitors from lima beans. Biochemistry, 2:66-71. With W. H. Stein. Relationships between structure and activity of ribonuclease. Proc.5th Int. Congr. Biochem., 4:33-38. Oxford: Pergamon Press. With A. M. Crestfield and W. H. Stein. Alkylation and identifica- tion of the histidine residues at the active site of ribonuclease. I. Biol. Chem., 238:2413 -20. With A. M. Crestfield and W. H. Stein. Properties and conforma- tion of the histidine residues at the active site of ribonuclease. J. Biol. Chem., 238:2421 - 28. A discussion of methods that have proved useful in research on ribonuclease. In: Aspects of Protein Structure, pp. 309-18. Lon- don: Academic Press. 1964 With S. Ota and W. H. Stein. Preparation and chemical properties of purified stem and fruit bromelains. Biochemistry, 3: 180-85. With D. C. Shaw and W. H. Stein. Inactivation of chymotrypsin by cyanate. I. Biol. Chem., 239:671-73. La structure et l'activite de la ribonuclease pancreatique. Bull. Soc. Chim. Biol., Suppl. 45:195-99.

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380 BIOGRAPHICAL MEMOIRS 1965 With T.-Y. Liu, W. H. Stein, and S. D. Elliott. The sequence of amino acid residues around the sulfhydryl group at the active site of streptococcal proteinase. I. Biol. Chem., 240:1143-49. With W. Ferdinand and At. H. Stein. An unusual disulfide bond in streptococcal proteinase. I. Biol. Chem. 240: 1150-55. With W. Ferdinand and W. H. Stein. Susceptibility of reduced, al- kylated trypsin inhibitors from lima beans to tryptic action. Biochim. Biophys. Acta, 96:524-27. With R. L. Heinrikson, A. M. Crestfield, and W. H. Stein. The reac- tivities of the histidine residues at the active site of ribonuclease toward halo acids of different structure. l. Biol. Chem., 240:2921-34. Experiments on disulfide bonds of proteins. III Congres Interna- tional de la Recherche Textile Laniere. Conferences Plenieres. pp. 53-60. Institut Textile de France, Paris. With B. I. Gerwin and W. H. Stein. On the specificity of strepto- coccal proteinase. l. Biol. Chem., 241:3331-39. With T. G. Rajagopalan and W. H. Stein. Pepsin from pepsinogen. Preparation and properties. I. Biol. Chem., 241:4940-50. With T. G. Rajagopalan and W. H. Stein. The inactivation of pep- sin by diazoacetyl-norleucine methyl ester. l. Biol. Chem., 241 :4295-97. 1967 With T. A. A. Dopheide and W. H. Stein. The carboxyl-terminal sequence of porcine pepsin. l. Biol. Chem., 242: 1833-37. With W. H. Stein and T.-Y. Liu. Structural studies of the proteinase from group A streptococci. Abstracts Vol., 7th Int. Congr. of Biochem., pp. 11-12. Tokyo. With K. Takahashi and W. H. Stein. The identification of a glu- tamic acid residue as part of the active site of ribonuclease To. i. Biol. Chem., 242:4682-90. 1968 With l. M. Manning. Determination of D- and L-amino acids by ion exchange chromatography as L-D and L-L dipeptides. }. Biol. Chem., 243:5591-97. With M. C. Lin and W. H. Stein. Further studies on the alkylation

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STANFORD MOORE 381 of the histidine residues at the active site of pancreatic ribonu- clease. J. Biol. Chem., 243:6167-70. Amino acid analysis: Aqueous dimethyl sulfoxide as solvent for the ninhydrin reaction. }. Biol. Chem., 243:6281-83. 1969 With P. A. Price, T.-Y. Liu, and W. H. Stein. Properties of chro- matographically purified bovine pancreatic deoxyribonuclease. I. Biol. Chem., 244:917-23. With P. A. Price and W. H. Stein. Alkylation of a histidine residue at the active site of bovine pancreatic deoxyribonuclease. J. Biol. Chem., 244:924-28. With P. A. Price and W. H. Stein. Effect of divalent cations on the reduction and reformation of the disulfide bonds of deoxyri- bonuclease. I. Biol. Chem., 244:929-32. With B. }. Catley and W. H. Stein. The carbohydrate moiety of bo- vine pancreatic deoxyribonuclease. i. Biol. Chem., 244:933-36. With R. L. Lundblad. Studies on the solubilization of 2',3'-cyclic nucleotide 3'-phosphohydrolase from bovine brain. Brain Res., 12:227-29. With }. M. Manning, W. B. Rowe, and A. Meister. Identification of l-methionine s-sulfoximine as the diastereoisomer of 1- methionine sr-sulfoximine that inhibits glutamine synthetase. Biochemistry, 8:2681-85. 1970 With M. Bustin, M. C. Lin, and W. H. Stein. Activity of the reduced zymogen of streptococcal proteinase. }. Biol. Chem., 245:846- 49. Streptococcal proteinase. In: Structure-Function Relationship of Pro- teolytic Enzymes, ed. P. Desnuelle, H. Neurath, and M. Ottesen, pp. 289-97. Copenhagen: Munksgaard. F With M. C. Lin, B. Gutte, and R. B. Merrifield. Regeneration of activity hv mixture of rihon~cle~se en7vmic~aliv degraded from _ . , _, ~ ~ _, , ~ _ . . . . ~ ~ ~ ~ ~ . . ~ ()H terminus and a synthetic cooti-term~nal tetracleca- peptide. I. Biol. Chem., 245:5169-70. With }. Salnikow and W. H. Stein. Comparison of the multiple forms of bovine pancreatic deoxyribonuclease. i. Biol. Chem., 245:5685-90.

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382 BIOGRAPHICAL MEMOIRS 1971 With B. V. Plapp and W. H. Stein. Activity of bovine pancreatic deoxyribonuclease A with modified amino groups. I. Biol. Chem., 246:939-45. 1972 With T. E. Hugli. Determination of the tryptophan content of pro- teins by ion exchange chromatography of alkaline hvdrolvsates. I. Biol. Chem., 247:2828-34. / J __ With M. C. Lin, B. Gutte, D. G. Caldi, and R. B. Merrifield. Reac- tivation of des(119-124) ribonuclease A by mixture with syn- thetic COOH-terminal peptides, the role of phenylalanine-120. I. Biol. Chem., 247:4768-74. The precision and sensitivity of amino acid analysis. In: Chemistry and Biology o:Peptides, ed. i. Meienhofer, pp. 629-53. Ann Ar- bor: Ann Arbor Science Publishers. 1973 With }. Salnikow, T.-H. Liao, and W. H. Stein. Bovine pancreatic deoxyribonuclease A. Isolation, composition, and amino acid sequences of the tryptic and chymotryptic peptides. J. Biol. Chem., 248:1480-88. With T.-H. Liao, }. Salnikow, and W. H. Stein. Bovine pancreatic deoxyribonuclease A. Isolation of cyanogen bromide peptides; complete covalent structure of the polypeptide chain. I. Biol. Chem., 248: 1489-95. With R. Hayashi and W. H. Stein. Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. i. Biol. Chem., 248:2296- 302. With W. H. Stein. Chemical structures of pancreatic ribonuclease and deoxyribonuclease. Les Prix Nobel en 1972, pp. 120-143. Stockholm: Nobel Foundation, and Science, 180:458-64. With R. Hayashi and R. B. Merrifield. Preparation of pancreatic ribonucleases 1-114 and 1-115 and their reactivation by mixture with synthetic COOH-terminal peptides. i. Biol. Chem., 248:3889-92. With T. E. Hugli and M. Bustin. Spectrophotometric assay of 2', Acyclic nucleotide 3'-phosphohydrolase: Application to the enzyme in bovine brain. Brain Res., 58:191-203.

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STANFORD M OORE 383 With R. Hayashi and W. H. Stein. Serine at the active center of yeast carboxypeptidase. I. Biol. Chem., 248:8366-69. 1974 With I. Bartholeyos. Pancreatic ribonuclease: Enzymic and physi- ological properties of a cross-linked dimer. Science, 186:444- 45. With J. Bartholeyns and W. H. Stein. A pancreatic ribonuclease active at pH 4.5. Int. l. Pept. Protein Res., 6:407-17. Lyman C. Craig, In Memoriam. Proc. 4th Am. Pept. Symp., ed. R. Walter and J. Meienhofer, pp. 5-16. Ann Arbor: Ann Arbor Science Publishers. With P. L. Fletcher, fir. Hydrolysis and cyclization of L-aspartyl-L- phenylalanine methyl ester in blood plasma in vitro. Proc. 4th Am. Pept. Symp., ed. R. Walter and J. Meienhofer, pp. 625- 631. Ann Arbor: Ann Arbor Science Publishers. With A. Guha. Solubilization of 2' ,3'-cyclic nucleotide 3'- phosphohydrolase from bovine brain without detergents. Brain Res., 89: 279-86. 1976 With D. Wang and G. Wilson. Preparation of cross-linked dimers of pancreatic ribonuclease. Biochemistry, 15 :660 - 65. Sulla ribonucliasi pancreatica. Rend. Atti Accad. Med. Chir., 129:250-58, Naples. 1977 With D. Wang. Polyspermine-ribonuclease prepared by cross- linkage with dimethyl suberimidate. Biochemistry, 16:2937-42. With P. Blackburn and G. Wilson. Ribonuclease inhibitor from hu- man placenta. Purification and properties. i. Biol. Chem., 252 :5904-10. With J. Bartholeyns, D. Wang, P. Blackburn, G. Wilson, and W. H. Stein. Explanation of the observation of pancreatic ribonu- clease activity at pH 4.5. Int. i. Pept. Protein Res., 10:172-75. 1978 150 Years ago: On the artificial formation of urea. Trends Bio- chem. Sci., 3:17-18. Lyman Creighton Craig, 1906 -1974. In: Biographical Memoirs of the

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384 BIOGRAPHICAL MEMOIRS National Academy of Sciences, vol. 49, pp. 49-77. Washington, D.C.: National Academy of Sciences. Chrornatographic procedures that are proving useful in research on ribonucleases. I. Chromatogr., 195:3 -12. With D. Wang. Preparation of protease-free and ribonuclease-free pancreatic deoxyribonuclease. l. Biol. Chem., 253:7216 -19. 1979 Chemical and biological experiments with pancreatic ribonuclease. Ital. I. Biochem., 28:297-99. Ernesto Scoffone Lecture, Biochemistry of derivatives of pan- creatic ribonuclease. Chim. Ind. Milan, 61:425. With W. H. Stein. An autobiographic memoir. In: i. Chromatogr. Library, vol. 17, 75 Years of Chromatography A Historical Dia- logue, ed. L. S. Ettre and A. Zlatkis, pp. 297-308. New York: Elsevier. 1980 With D. Giulian. Identification of 2' ,3'-cyclic nucleotide 3'- phosphodiesterase in the vertebrate retina. I. Biol. Chem., 255:5993 -95. W. H. Stein. J. Biol. Chem., 255:9517-18. William H. Stein's achievements as a scientist. Montefiore Med., 5 (2~:36-38. With L. E. Burton and P. Blackburn. Ribonuclease inhibitor from bovine brain. Int. }. Pept. Protein Res., 16:359-64. Introductory review to a symposium concerned with forty years of research on proteins. In: The Evolution of Protein Structure and Function, ed. D. S. Sigman and M. A. B. Brazier, pp. 1-19. New York: Academic Press. 1981 Pancreatic DNase. In: The Enzymes, ed. P. Boyer, vol. 14, pp. 281- 96. New York: Academic Press. Dedication to William H. Stein. In: Chemical Synthesis and Sequencing of Peptides and Proteins, ed. T.-Y. Liu, A. N. Schechter, R. L. Heinrickson, and P. G. Collide, pp. 17-25. Amsterdam: E1- sevier North Holland Biomedical Press B.V.

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STANFORD MOORE 1982 385 With P. Blackburn. Pancreatic ribonucleases. In: The Enzymes, ed. P. Boyer, vol. 15, pp. 317-433. New York: Academic Press. With K. Takahashi. Ribonuclease To. In: The Enzymes, ed. P. Boyer, vol. 15, pp. 435-68. New York: Academic Press. 1986 William H. Stein, 1911-1980. In: Biographical Memoirs of the Na- tional Academy of Sciences, vol.56, pp.415 - 39. Washington, D.C.: National Academy Press.