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Biographical Memoirs: Volume 63 This page in the original is blank.
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Biographical Memoirs: Volume 63 NATHAN ORAM KAPLAN June 25, 1917–April 15, 1986 BY W. D. MCELROY NATHAN ORAM KAPLAN was born in New York City on June 25, 1917. When he was two years old his family moved to Los Angeles where, after attending primary and secondary schools, he entered UCLA to major in chemistry. After graduating from UCLA he went to Berkeley for graduate studies. Until this time, Nate's main interests were in baseball and track. He ran the quarter mile and was a member of the track team at UCLA. However, he was also interested in the history of science writing, for which he received an award from the city of Los Angeles. At Berkeley, Nate's latent talents in research were uncovered and he virtually exploded into recognition. Working in Professor David M. Greenberg's laboratory, he used radioactive phosphate, produced by Martin D. Kamen (a lifetime friend and colleague) with the cyclotron at the Radiation Laboratory, to study phosphate metabolism in rat liver. As he developed experience with radioactive phosphate, he established a collaboration with M. Doudoroff and W. Z. Hassid, two young bacteriologists who were studying phosphate-dependent sucrose degradation by an enzyme from Pseudomonas sacchraphila. With Nate's help, they established that the enzyme transferred the glucosyl moiety
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Biographical Memoirs: Volume 63 of sucrose to radioactive phosphate. Since this was the first demonstration of a sugar transfer reaction, Doudoroff and Hassid were recipients of the Sugar Research Award, the monetary part of which they shared with Nate. World War II interrupted Nate's research career in biochemistry. From 1942 until 1945 he worked as a research chemist on the Manhattan Project. In 1945, when Nate attended an American Chemical Society meeting in New York, one of his relatives arranged a blind date for him and the couple met on the steps of the 42nd Street library. This was the first meeting of Nate and Goldie. Soon afterward Nate joined Fritz Lipmann's laboratory at the Massachusetts General Hospital. Every other weekend Nate would travel from Boston to New York to see Goldie and over the Thanksgiving weekend of 1947, Goldie agreed to marry him. This worried Lipmann, who thought that Goldie might be a "wild New Yorker." Nate's research career flourished under the influence of Lipmann. During his time at Mass General he isolated coenzyme A, was instrumental in determining its structure, and helped establish the universality of coenzyme A in "two-carbon" metabolism. For this and earlier work that led to the discovery of coenzyme A, Lipmann shared the Nobel Prize in Physiology and Medicine in 1953. For his contributions to the work on coenzyme A, Nate shared the Nutrition Award in 1948 and received the Eli Lily Award in Biochemistry in 1953. Nate left Lipmann's laboratory in 1950 to become assistant professor of biochemistry at the University of Illinois Medical School in Chicago, primarily because Sidney Colowick, who had just left the Cori laboratory at Washington University in St. Louis, was there. Problems developed for Colowick and Kaplan at Illinois and they were both hired
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Biographical Memoirs: Volume 63 (by W. D. McElroy) as assistant professors at the McCollum-Pratt Institute of the Department of Biology of Johns Hopkins University. At Hopkins, Nate and Sidney developed a successful and productive collaboration studying the chemistry of the pyridine nucleotide coenzymes and the enzymes that are involved with them. This collaboration led to the founding in 1955 of the classic series, Colowick and Kaplan's Methods in Enzymology, which now has more than 140 volumes with more in press. In 1957 Nate left Johns Hopkins University to become founding chairman of the Graduate Department of Biochemistry at Brandeis University. To establish the new department he, in association with Martin Kamen who joined him at Brandeis, hired about a dozen carefully selected young assistant professors and brought them to a campus where very little space was available for them for at least a year. Under these conditions and with Nate as catalyst, an uncommon camaraderie developed between faculty, postdoctoral fellows, graduate students, and staff that led to scientific productivity of such caliber that his fledgling department gained international recognition in a very short time. By recognition for his department, Nate Kaplan played a major role in establishing Brandeis, which had only been founded in 1948, as a major, research oriented university in the sciences in the 1960s. His research at Brandeis was primarily concerned with the structure-function relationships of dehydrogenases, which led him into the areas of enzyme evolution and isoenzymes. He was one of the first to recognize the potential of using isoenzymes analysis in clinical diagnosis and for this reason developed methods for detecting lactate dehydrogenase isoenzymes in human serum. In 1968, pulled by the urgings of Martin Kamen who
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Biographical Memoirs: Volume 63 had already come to USD, and pushed by circumstances of campus politics at Brandeis, Nate joined the Chemistry Department. His appointment and laboratories were in the School of Medicine. He was drawn to the medical school environment by his earlier association with Fritz Lipmann at Massachusetts General Hospital and his collaboration with Abraham Goldin of the National Institutes of Health in cancer chemotherapy, which dated back to his years at Johns Hopkins in the 1950s. In the 1970s, he and Gordon Sato established a successful colony of athymic mice. The mice were used to examine anti-cancer agents making this facility an important component of the UCSD Cancer Center. Nate's laboratory also made important contributions in more traditional areas of biochemical research at UCSD. Using NMR, his students and postdoctoral fellows established the conformations of the pyridine nucleotide coenzymes and other nucleotides in aqueous solution. Other important contributions were on the development of matrices for affinity chromatography of enzymes, immobilization of enzymes, and immobilization of ligands for membrane receptors. What transcends his scientific accomplishments was the warm and inspiring influence that Nate Kaplan had on those who worked with him. Young investigators from the world over were drawn to his laboratory, where they were accommodated with excellent research problems, excellent facilities, and the qualities of the man himself. These qualities were a combination of warmth, understanding, keen insight, and a contagious enthusiasm for biochemistry which permeated all of his professional activities. Throughout the years from 1945 on, Goldie was supportive, not only as a loving wife, but also as a companion who accompanied Nate to meetings the world over. She proofread and gave
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Biographical Memoirs: Volume 63 finishing touches to the numerous manuscripts that crossed his desk. Nate shared with Goldie the many problems of a varied career and she responded with good advice for calm and reason in seasons of turbulence. Nate's interests in biochemistry were very broad and included biochemical anthropology, the topic of a popular course that he taught. In the late 1960s and 1970s, partly out of his enthusiasm to learn more about particular aspects of biochemical anthropology, many of his family vacation journeys with Goldie and their son Jerrie ended up in remote places where he could observe, firsthand, social practices that had evolved in response to biochemical defects in the food supply or in the human population itself. During his career, Nate Kaplan had enormous impact on the field of biochemistry and profound influence on his many associates in this country and abroad. He is deeply missed. Martin Kamen has written a brief account of Nate's stay at Berkeley. "At the Radiation Laboratory, led by the charismatic Ernest Laurence, the Cyclotron was pouring out an unprecedented flood of radioactive isotopes for use in biological research. Some of his prospective customers were concentrated in the western end of the campus—the Life Sciences Building. Among them were soil scientists (H. A. Barker and W. Z. Hassid), bacteriologists (notably M. Doudoroff), and other groups in biochemistry (under the aegis of David Greenberg) and physiology (led by I. Chaikoff)." This was where Martin first met Nate. In the meantime, Nate had moved from the Chemistry Department to Biochemistry, where he was working with Greenberg on phosphorous metabolism for his Ph.D. dissertation. Here he met Doudoroff, Hassid, and Barker. Barker has recalled these events. "Doudoroff had been studying the utiliza-
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Biographical Memoirs: Volume 63 tion of various sugars by Pseudomonas sacchraphila so called because it oxidizes sucrose much more rapidly than the constituent monosaccharides, glucose and fructose. Suspensions of dried cells of the organism were found to decompose sucrose more rapidly in the presence than in the absence of inorganic phosphate." Doudoroff, Kaplan, and Hassid worked together to demonstrate that glucose-1-phosphate and fructose were the products of sucrose breakdown. These results were published in 1943 in the Journal of Biological Chemistry; the article was Nate's first scientific publication. After Nate received his Ph.D., he went to work with Fritz Lipmann at the Massachusetts General Hospital. Mary Ellen Jones has recounted these events. "At the time Lipmann's laboratory was small, only three people, Lipmann, Kaplan and a technician/secretary, L. Constance Tuttle. Lipmann had recently shown that the acetylation of sulfanilamide by pigeon liver extracts required a heat-stable factor which was autolyzed when the extract stood for several hours at room temperature. Kaplan began to purify the factor, now known as coenzyme A, using the restoration of enzyme activity to aged extracts as a measure of the amount of cofactor present." Nate, working with G. David Novelli and Beverly Guirard, soon found that the cofactor contained pantothenic acid, and later Shuster and Kaplan found that a phosphate group was attached to the 3¢-hydroxyl of the ribose ring of adenylic acid. In the meantime Kaplan and Lipmann found that most of the pantothenate in tissues was present in coenzyme A. The time Nate spent with Lipmann was a great learning experience and influenced Nate's outlook on scientific research for the rest of his life. Nate Kaplan and I had been friends and colleagues since 1950. The nature of our meeting was very unusual. In
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Biographical Memoirs: Volume 63 1947, Mr. John Lee Pratt had donated a sum of money to start a center for the study of trace metals in biological systems at the Johns Hopkins University. I was an assistant professor in biology at the time, but for some reason, Dr. E. V. McCollum convinced President I. Bowman that I should be given the charge to describe what this new center should do scientifically. At the time very little dynamic biochemistry was being taught, either in the graduate or medical schools in the United States. In other words, there was a large gap between European–English biochemistry and that of the United States. Only in 1941 when Lipmann and Kalckar published their famous reviews was ATP introduced widely in the U.S. biochemical literature. Phosphorus was a macronutrient! I was convinced that a new approach looking at the dynamic functions of metals in enzyme systems was the way to go, so I wrote up a four-or five-page outline of the program and gave it to Dr. McCollum. Six outstanding nutritional scientists from England, Australia, New Zealand, and the United States, and two enzymologists were invited to Hopkins to discuss this proposal. Interestingly enough, they agreed with the plan and, subsequently, I was asked to propose names for the directorship. I submitted the names of a number of outstanding enzymologists, including Dr. Sidney Colowick. Unfortunately, most were not interested in the function of trace elements in enzyme function and metabolic processes in general and, unfortunately, right after the war there were not many enzymologists looking for jobs, so we had no takers. After a year things appeared to be desperate, and Dr. McCollum, without consulting me, convinced President Bowman that I should be named director of the center, which we subsequently named the McCollum–Pratt Institute. Within a few weeks after I assumed the directorship, I had a call
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Biographical Memoirs: Volume 63 from Dr. Stanley Carson at the Oak Ridge National Laboratories indicating that Dr. Colowick might be available. I immediately called Sid and made him an offer. The next day he returned my call and said he was interested if he could bring a young associate named N. O. Kaplan. I invited both of them to visit Hopkins, and they arrived within two days. That was the first time I met Nate Kaplan. Within two weeks I had all the paperwork finished and approved by the Academic Senate, the dean, and the president. To this day it is the fastest appointment that I have ever made, and they readily accepted. It is interesting that there are no letters on file concerning the qualifications of Nate, only a phone call from Fritz Lipmann and Mike Doudoroff. What a wonderful way to make an appointment; they were two of the best I ever made. The original members of the McCollum–Pratt, in addition to myself, were Kaplan, Colowick, the late Alvin Nason, Henry Little, and Robert Ballentine. We were housed in a greenhouse on the Homewood campus. There were two large laboratories on the first floor. Nate and Sid shared one, and the other three shared the second. My labs were in the Biology Department about two minutes from the greenhouse. It was not the best of arrangements as we know them today, but it turned out to be a very scientifically productive environment. Housed in the basement was Dr. Elmer V. McCollum, who had just retired as chairman of the Department of Biochemistry in the School of Hygiene at Johns Hopkins. He and Nate became very close friends. With Nate's interest in history, he spent hours in the basement learning all he could about the history of nutrition and biochemistry from Dr. McCollum. It is interesting that the year that Warburg discovered the requirement of Mg2+ for the triose phosphate dehydrogenase was
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Biographical Memoirs: Volume 63 the same year that McCollum demonstrated it as an essential micronutrient in animals. In this environment, Nate was "all ears," and it had a great influence on his teaching of biochemistry in later years. I never asked Nate or Sid to be concerned with trace metal biochemistry, but I was reasonably sure how it would work out, because when bright people work side by side, things happen. The plan was to bring young postdoctoral students from laboratories where nutritional trace element work was being performed. Dr. Alvin Nason and I agreed to work with them on enzymological problems. At the time, I had a number of nitrate mutants in Neurospora that could reduce nitrate to nitrite, but the latter would not be further metabolized. There were reasons to suspect that molybdenum might be involved in the nitrate reductase reaction, so we invited Dr. D. J. D. Nicholas from Long Ashton, England, to join us in this research; he was an expert on removing trace metals from proteins and growth medium. After about six months, we had drawn a blank. Then one day, while talking with Nate, he suggested trying FAD instead of FMN as an electron donor. Fortunately, Nate had some FAD in the deep freeze, and the first time we tried it, we found that TPNH (NADPH) would reduce the nitrate to nitrite. This, of course, led to the eventual discovery that reduced FAD was the immediate electron donor for the reduction of molybdenum and subsequently the reduction of nitrate. So Nate was into trace metal metabolism! Demonstrating that the proximity of two types of investigators often leads to an exchange of ideas, techniques, and materials that is of great mutual benefit. This was one of Nate's great assets. He was willing to help anyone in need—graduate students, postdocs, faculty and visiting scientists, and an undergraduate looking for a
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Biographical Memoirs: Volume 63 problem. It is interesting that Dr. David Greenberg recalls that when Nate worked with him on war research Nate "had no interest in mineral metabolism. He used 32P to study various aspects of carbohydrate metabolism." Molybedenum was not the only trace element problem that Nate worked on. At the time, Al Nason was working on tryptophan metabolism in the zinc-deferent Neurospora. Without going into detail, this led to the discovery of an interesting and potent DPNase, which increased dramatically in zinc-deficient mycelia. It turned out to be very stable and easy to purify, in contrast to the mammalalian DPNases. Following the discovery of Neurospora DPNase, Nate and Sid continued their work together on various aspects of this and other enzymes concerned with DPN, particularly the exchange reactions involving ADP ribosyl enzyme and various nicotinamide derivatives. The best known of these was the acetylpyridine analog, which was very active as a coenzyme in many dehydrogenases. The ratio of the activity with DPN and the acetylpyridine analog was a very sensitive measure of the differences of various dehydrogenases in different species and in different organs. I believe this work was the basis for Nate becoming interested in evolution. He studied the isozymes of various dehydrogenases and noted their changes during development. Probably his best-known work in the area was concerned with the M and H isozymes of lactic dehydrogenase, this latter work leading to his interest in cancer metabolism. It was from this interesting work that Nate really became a biologist. Working on lactic dehydrogenases from various crabs, he found that the horseshoe crab (Limmulus) did not fit the general properties of other crabs. Fortunately his asso-
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Biographical Memoirs: Volume 63 otide and related pyridinium slats with alkali. Arch. Biochem. Biophys. 101 (139). 1964 With Amadeo Pesce, Robert H. McKay, Francis Stolzenbach, and Robert D. Cahn. The comparative enzymology of lactic dehydrogenases. I. Properties of the crystalline beef and chicken enzymes. J. Biol. Chem. 239:1753–61. With William S. Allison. The comparative enzymology of triosephosphate dehydrogenase. J. Biol. Chem. 239:2140–52. With Robert D. Goldman and Thomas C. Hall. Lactic dehydrogenase in human neoplastic tissue. Cancer Res. 24:389–98. With David M. Dawson and Theodore L. Goodfriend. Lactic dehydrogenase: Function of the two types. Science 143:929–33. With Thomas P. Fondy, Amadeo Pesce, Irwin Freedberg, and Francis Stolzenbach. The comparative enzymology of lactic dehydrogenases. II. Properties of the crystalline HM3 hybrid from chicken muscle and of H2M2 hybrid and H4 enzyme from chicken liver. Biochemistry 3:522–30. With William S. Allison. Effect of tetrathionate on the stability and immunological properties of muscle triosephosphate dehydrogenases. Biochemistry 3:1792–1800. With Takashi Kawasaki and Kenshi Satoh. The involvement of pyridine nucleotide transhydrogenase in ATP-linked TPN reduction by DPNH. Biochem. Biophys. Res. Commun. 17:648–54. 1965 With Giovanni Di Sabato. The denaturation of lactic dehydrogenases. II. The effect of urea and salts. J. Biol. Chem. 240:1072–76. With Oscar P. Chilson and Louis A. Costello. Studies on the mechanism of hybridization of lactic dehydrogenases in vitro. Biochemistry 4:271–81. With Oscar P. Chilson and G. Barrie Kitto. Factors affecting the reversible dissociation of dehydrogenases. Proc. Natl. Acad. Sci. USA 53:1006–14. With Stanley N. Salthe and Oscar P. Chilson. In vivo and in vitro hybridization of lactic dehydrogenases. Nature 207:723–28. With David M. Dawson and Hans M. Eppenberger. Creatine kinase:
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Biographical Memoirs: Volume 63 Evidence for a dimeric structure. Biochem. Biophys. Res. Commun. 21:346–53. With Theodore L. Goodfriend. Isoenzymes in clinical diagnosis. Circulation 32:1010–20. With Stanley N. Salthe. Comparative catalytic studies of lactic dehydrogenase in the amphibia: Environmental and physiological correlations. Comp. Biochem. Physio. 16:393–408. 1966 With G. Barrie Kitto, Paul M. Wassarman, and Jan Michjda. Multiple forms of mitochondrial malate dehydrogenases. Biochem. Biophys. Res. Commun. 22:75–81. With Audrey E. Evans. Pyridine nucleotide transhydrogenase in normal human and leukemic leukocytes. J. Clin. Invest. 45:1268–72. With Stanley N. Salthe. Immunology and rates of enzyme evolution in the amphibia in relation to the origins of certain taxa. Evolution 20:603–16. With G. Barrie Kitto and Allan C. Wilson. Evolution of malate dehydrogenase in birds. Science 153:1408–10. With Giovanni Di Sabato. The hydrogen ion equilibria of chicken heart lactic dehydrogenase . Biochemistry 5:3980–86. 1967 With Norbert I. Swislocki, Martin I. Kalish, and Fred I. Chasalow. Solubilization and comparative properties of some mammalian diphosphopyridine nucleotidases. J. Biol. Chem. 242:1089–94. With W. H. Murphy. Malate dehydrogenases. III. Alteration of catalytic properties during purification of Bacillus subtilis malate dehydrogenases. J. Biol. Chem. 242:1560–66. With Amadeo Pesce, Thomas P. Fondy, Francis Stolzenbach, and Fred Castillo. The comparative enzymology of lactic dehydrogenases. III. Properties of the H4 and M4 enzymes from a number of vertebrates. J. Biol. Chem. 242:2151–67. With Leonard Corman. Kinetic studies of dogfish liver glutamate dehydrogenase with diphosphopyridine nucleotide and the effect of added salts. J. Biol. Chem. 242:2840–47. With David M. Dawson and Hans M. Eppenberger. The comparative enzymology of creatine kinases. II. Physical and chemical properties. J. Biol. Chem. 242:210.
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Biographical Memoirs: Volume 63 With Sandra L. Blethen. Purification of arginine kinase from lobster and a study of some factors affecting its reactivation. Biochemistry 6:1413–21. With M. E. Eppenberger and H. M. Eppenberger. Evolution of creatine kinase. Nature 214:239–43. With G. Barrie Kitto, Margaret E. Kottke, Linda H. Bertland, and William H. Murphy. Studies on malate dehydrogenases and aspartate aminotransferases from Neurospora crassa. Arch. Biochem. Biophys. 121:244–52. With J. J. Herskovits, C. J. Masters, and P. M. Wassarman. On the tissue specificity and biological significance of aldolase C in the chicken. Biochem. Biophys. Res. Commun. 26:24–29. 1968 With Paul M. Wassarman. Iodination of muscle fructose diphosphate aldolase. J. Biol. Chem. 243:720–29. With E. M. Tarmy. Chemical characterization of D-lactate dehydrogenase from Escherichia coli B. J. Biol. Chem. 243:2579–86. With Ramaswamy H. Sarma. 220 MHz nuclear magnetic resonance spectra of oxidized and reduced pyridine dinucleotide. J. Biol. Chem. 244:771–74. With Arnold I. Caplan and Edgar Swilling. 3-acetyl-pyridine effects in vitro related to teratogenic activity in chicken embryos. Science 160:1090–91. With Linda H. Bertland. Chicken heart soluble aspartate aminotransferase. Purification and properties. Biochemistry 7:134–42. With Sandra L. Blethen. Characteristics of arthropod arginine kinases. Biochemistry 7:2123–35. With Ramaswamy H. Sarma and Priscilla Dannies. Investigation of inter-and intramolecular interactions in flavin-adenine dinucleotide by proton magnetic resonance. Biochemistry 7:4359–67. With Regina Pietruszko and Howard J. Ringold. Antibody studies with the multiple enzymes of horse liver alcohol dehydrogenase II. Biochem. Biophys. Res. Commun. 33:503–7. 1969 With F. Kaplan and P. Setlow. Purification and properties of a DPNH-TPNH diaphorase from Clostridium kluyverii. Arch. Biochem. Biophys. 132:91–98.
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Biographical Memoirs: Volume 63 With Harry D. Kaloustian. Lactate dehydrogenase of lobster (Homarus Americanus) tail muscle. II. Kinetics and regulatory properties. J. Biol. Chem. 244:2902–10. With William S. Allison and Jan Admiraal. The subunits of dogfish M4 lactic dehydrogenase. J. Biol. Chem. 244:4743–49. With C. R. Roe and K. S. You. Agar gel electrophoretic demonstration of charge alteration in mutant bacterial proteins. Biochem. Biophys. Res. Commun. 36:64–74. With R. H. Sarma. 220 MHz proton nuclear magnetic resonance study of the geometic disposition of the base pairs in the oxidized and reduced pyridine nucleotides. Biochem. Biophys. Res. Commun. 36:780–89. With Charles R. Roe. Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases. Biochemistry 8:5093–103. 1970 With R. H. Sarma. High frequency nuclear magnetic resonance study of the M and P helices of reduced pyridine dinucleotides. Biochemistry 9:539–48. With Johannes Everse, David A. Gardner, Wladyslaw Galasinksi, and Kivie Moldave. The formation of a ternary complex between diptheria toxin, aminoacetyltransferase II and diphosphopyridine nucleotide. J. Biol. Chem. 245:899–901. With Daniel Louis. Stereospecificity of hydrogen transfer reactions of the Pseudomonas aeruginosa pyridine nucleotide transhydrogenase. J. Biol. Chem. 245:5691–98. With R. H. Sarma. 220 MHz proton nuclear magnetic resonance study of the interaction between chicken M4 lactate dehydrogenase and reduced diphosphopyridine nucleotide. Proc. Natl. Acad. Sci. USA 67:1375–82. 1971 With A. S. Levi. The role of reduced diphosphopyridine nucleotide in the reactivation of dogfish muscle lactate dehydrogenase. Biochem. Biophys. Res. Commun. 45:1615–21. With N. J. Oppenheimer and L. J. Arnold. A structure of pyridine nucleotides in solution. Proc. Natl. Acad. Sci. USA 68:3200–05.
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Biographical Memoirs: Volume 63 1972 With G. S. Sensabaugh. A lactate dehydrogenase specific to the liver of gadoid fish. J. Biol. Chem. 247:585–93. With D. A. Gardner and G. H. Sato. Pyridine nucleotides in normal and nicotinamide depleted adrenal tumor cell cultures. Dev. Biol. 28:84–93. With M. Raszka. Association by hydrogen bonding of mononucleotides in aqueous solution. Proc. Natl. Acad. Sci. USA 69:202–6. With J. C. Venter, J. E. Dixon, and P. R. Maroko. Biologically active catecholamines covalently bound to glass beads. Proc. Natl. Acad. Sci. USA 69:1141–45. 1973 With George L. Long. Diphosphopyridine nucleotide-linked D-lactate dehydrogenases from the horseshoe crab, Limulus polyphemus and the seaworm, Nereis virens. I. Physical and chemical properties. Arch. Biochem. Biophys. 154:696–701. With Ronald R. Fisher. Studies on the mitochondrial energy-linked pyridine nucleotide transhydrogenase. Biochemistry 12:1182–88. With J. Craig Venter, John Ross, Jr., Jack E. Dixon, and Steven E. Mayer. Immobilized catecholamine and cocaine effects on contractility of cardiac muscle. Proc. Natl. Acad. Sci. USA 70:1214–17. With S. S. Taylor, S. S. Oxley, and W. S. Allison. Aminoacid sequence of dogish M4 lactate dehydrogenase. Proc. Natl. Acad. Sci. USA 70:1790–93. With John R. Benemann, Jeffrey A. Berenson, and Martin Kamen. Hydrogen evolution by a chloroplast–ferredoxin–hydrogenase system. Proc. Natl. Acad. Sci. USA 70:2317–20. With Norman J. Oppenheimer. The primary acid product of DPNH. Biochem. Biophys. Res. Commun. 50:683–90. With Jack E. Dixon, Francis E. Stolzenbach, and Jeffrey A. Berenson. Immobilized enzymes: The catalytic properties of lactate dehydrogenase covalently attached to glass beads. Biochem. Biophys. Res. Commun. 52:905–12. With Bernard Witholt. Methods for isolating mutants overproducing nicotinamide adenine dinucleotide and its precursors. J. Biol. Chem. 109:350–74. 1974 With L. J. Arnold. The structure of the abortive diphosphopyridine
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Biographical Memoirs: Volume 63 nucleotide-pyruvate-lactate dehydrogenase ternary complex as determined by proton magnetic resonance analysis. J. Biol. Chem. 249:652–55. With J. C. Venter, M. S. Yong, and J. B. Richardson. Stability of catecholamines immobiled on glass beads. Science 185:459–62. With Chi-Yu Lee and Norman J. Oppenheimer. Proton relaxation studies of diphosphopyridine coenzymes. Biochem. Biophys. Res. Commun. 60:838–43. With Johannes Everse, Jack E. Dixon, Francis E. Stolzenbach, Chi-Yu Lee, Ching-Lun T. Lee, Susan S. Taylor, and Klaus Mosbach. Purification and separation of pyridine nucleotide-linked dehydrogenases by affinity chromatography techniques. Proc. Natl. Acad. Sci. USA 71:3450–54. With Edward J. Pastore, Roy L. Kisliuk, Laurence T. Plante, and John M. Wright. Conformational changes induced in dihydrofolate reductase by folates, pyridine nucleotide coenzymes and methotrexate. Proc. Natl. Acad. Sci. USA 71:3849–53. With Matthew Raszka. Mononucleotides in aqueous solution: Proton magnetic resonance studies of amino groups. Biochemistry 13:4616–22. With Norman J. Oppenheimer. Glyceraldehyde-3-phosphate dehydrogenase catalyzed hydration of the 5-6 double bond of reduced [beta symbol]-nicotinamide adenine dinucleotide ([beta] NADH). Formation of [beta]-6-hydroxy-1, 4, 5, 6-tetrahydronicotinamide adenine dicnucleotide. Biochemistry 13:4685–93. 1975 With J. Craig Venter and Lyle J. Arnold, Jr. The structure and quantitation of catecholamines covalently bound to glass beads. Mol. Pharmacol. 11:1–9. With J. Craig Venter, Barbara R. Venter and Jack E. Dixon. A possible role for glass bead immobilized enzymes as therapeutic agents (immobilized uricase as enzyme therapy for hyperuricemia). Biochem. Med. 12:79–91. With Norman J. Oppenheimer. The alpha beta epimerization of reduced nicotinamide adenine dinucleotide. Arch. Biochem. Biophys. 166:526–35. With Alan S. Levi. Properties of water-insoluble matrix-bound lactate dehydrogenase. Arch. Biochem. Biophys. 169:115–21.
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Biographical Memoirs: Volume 63 With Johannes Everse and James B. Griffin. The pyridine nucleosidase from Bacillus subtilis. Kinetic properties and enzyme–inhibitor interactions. Arch. Biochem. Biophys. 169:714–23. With Chi-Yu Lee and Matthew J. Raszka. Determination of solution structure of diphosphopyridine coenzymes with paramagnetic shift and broadening reagents. J. Magn. Reson. 17:151–60. With J. Craig Venter and John Ross, Jr. Lack of detectable change in cyclic AMP during the cardiac inotropic response to isoproterenol immobilized in glass beads. Proc. Natl. Acad. Sci. USA 72:824–29. With Susan S. Taylor and William S. Allison. The amino acid sequence of the tryptic peptides isolated from dogfish M4 lactate dehydrogenase. J. Biol. Chem. 250:8740–49. 1976 With E. J. Pastore, L. T. Plante, J. M. Wright, and R. L. Kisliuk. Interaction of 13C-enriched folate with dihydrofolate reductase studied by carbon magnetic resonance spectroscopy. Biochem. Biophys. Res. Commun. 68:471–76. With Douglas A. Lappi, Francis E. Stolzenbach, and Martin D. Kamen. Immobilization of hydrogenase on glass beads. Biochem. Biophys. Res. Commun. 69:878–84. With Michael S. Verlander, J. Craig Venter, Murray Goodman, and Bernie Sacs. Biological activity of catecholamines covalently linked to synthetic polymers: Proof of immobilized drug theory. Proc. Natl. Acad. Sci. USA 73:1009–13. With Barbara R. Venter and J. Craig Venter. Affinity isolation of cultured tumor cells by means of drugs and hormones covalently-bound to glass and sepharose beads. Proc. Natl. Acad. Sci. USA 73:2013–17. With L. H. Lazarus, C.-Y. Lee, and B. Wermuth. Application of general ligand affinity chromatography for the mutual separation of deoxyribonuclease and ribonuclease free of protease contamination. Anal. Biochem. 74:138–44. With N. J. Oppenheimer. Proton magnetic resonance study of the intramolecular association and conformation of the [alpha symbol] and [beta symbol] pyridine mononucleotides and nucleotides. Biochemistry 15:3981–89. With F. Widmer. Regulatory properties of the pyridine nucleotide
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Biographical Memoirs: Volume 63 transhydrogenase from Pseudomonas aeruginosa. Kinetic studies and flourescence titration. Biochemistry 15:4693–99. With L. J. Arnold, Jr., Kwan-sa You, and W. S. Allison. Determination of the hydride transfer stereospecificity of nicotinamide adenine denucleotide-linked oxidoreductases by proton magnetic resonance. Biochemistry 15:4844–49. With B. R. Venter. Diptheria toxin effects on human cells in tissue culture. Cancer Res. 36:4590–94. 1977 With K.-S. You and L. J. Arnold, Jr. The stereospecificity of bacterial external flavorprotein monoxygenases for nicotinamide adenine dinucleotide . Arch. Biochem. Biophys. 180:550–54. With R. D. Eichner. Physical and chemical properties of lactate dehydrogenase in Homarus americanus. Arch. Biochem. Biophys. 181:490–500. With J. Everse, D. A. Lappi, J. M. Beglau, and C.-Y. Lee. Investigations into the relationship between structure and function of diphtheria toxin. Proc. Natl. Acad. Sci. USA 74:472–76. With T. Kakuno and M. D. Kamen. Chromatium hydrogenase. Proc. Natl. Acad. Sci. USA 74:861–63. 1978 With N. J. Oppenheimer and L. J. Arnold. Stereospecificity of the intramolecular association of reduced pyridine coenzymes. Biochemistry 17:2613–19. With P. E. Brodelius and R. A. Lannom. The synthesis of 8-(6-aminohexyl)-amino-GMP and its applications as a general ligand in affinity chromatography. Arch. Biochem. Biophys. 188:228–31. With P. E. Brodelius. Guanosine nucleotide analogues as general ligands in affinity chromatography. Enzyme Engineering 4:445–47. With A. M. Klibanov and M. D. Kamen. A rationale for stabilization of oxygen labile enzymes: Application to a Chostridial hydrogenase. Proc. Natl. Acad. Sci. USA 75:3640–43. 1979 With Frederick E. Evans. 31P nuclear magnetic resonance studies on relaxation parameters and line broadening of intracellular metabolites of HeLa cells. Arch. Biochem. Biophys. 193:63–75.
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Biographical Memoirs: Volume 63 With Peter E. Brodelius. Studies of bovine liver glutamate dehydrogenase by analytical affinity chromatography on immobilized AMP analogs. Arch. Biochem. Biophys. 194:449–56. With L. J. Arnold, Jr., A. Dagan, and J. Gutheil. Antineoplastic activity of ply-1-lysine with some ascites tumor cells. Proc. Natl. Acad. Sci. USA 76:3246–50. With G. Beattie, R. Lannom, J. Lipsick, and A. G. Osler. Streptozotocin-induced diabetes in athymic and conventional BALB/c mice. Diabetes 29:146–50. With A. Klibanov and M. D. Kamen. Chelating agents protect hydrogenase against oxygen inactivation. Biochim. Biophys. Acta 547:411–16. 1980 With W. P. MacConnell. The role of ethanol extractable proteins from the 80S rate liver ribosome. Biochem. Biophys. Res. Commun. 92:46–52. With B. R. Venter and L. M. Reid. Growth of human breast carcinomas in nude mice and subsequent establishment in tissue culture. Cancer Res. 40:95–100. With G. Beattie, S. Baird, R. Lannom, S. Slimmer, and F. C. Jensen. Induction of lymphoma in athymic mice: A model for study of the human disease. Proc. Natl. Acad. Sci. USA 77:4971–74. With F. E. Evans and J. M. Wright. Proton and phosphorus-31 nuclear magnetic resonance study on the stabilization of the anticonformation about the glycosyl bond of 8-alkylamino adenyl nucleotides. Biochemistry 19:2113–17. With A. F. Knowles. Oxidative phosphorylation and ATPase activities in human tumor mitochondria. Biochim. Biophys. Acta 590:170–81. With Alexander M. Klibanov and Martin D. Kamen. Thermal stabilites of membrane-bound, solubilized and artificially-immobilized hydrogenase from chromatium vinosum. Arch. Biochem. Biophys. 199:545–49. 1981 With F. C. Giuliani and K. A. Zirvi. Therapeutic response of human tumor xenografts in athymic mice to doxorubicin. Cancer Res. 41:325–35.
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Biographical Memoirs: Volume 63 With A. F. Knowles and J. F. Leis. Isolation and characterization of plasma membranes from transplantable human astrocytoma, oat cell carcinoma and melanomas. Cancer Res. 41:4031–37. With M. DeLuca, N. Hall, and R. Rice. Creatine kinase isozymes in human tumors. Biochem. Biophys. Res. Commun. 99:189–95. With A. F. Knowles. Variable ATPase composition of human tumor plasma membranes. Biochem. Biophys. Res. Commun. 99:1443–48. With S. M Shan, A. M. Klivanov, and M. D. Kamen. The effect of electron carriers and other ligands on oxygen stability of Clostridial hydrogenase. Biochim. Biophys. Acta 659:457–65. 1982 With S. M. Baird, G. M. Beattie, R. A. Lannom, J. S. Lipsick, and F. C. Jensen. Induction of lymphoma in antigenically-stimulated athymic mice. Cancer Res. 42:198–206. With W. P. MacConnell. The activity of the acidic phosphoproteins from the 80S rate liver ribosome. J. Biol. Chem. 257:5359–66. With G. M. Beattie, A. F. Knowles, F. C. Jensen, and S. M. Baird. Induction of sarcomas in athymic mice. Proc. Natl. Acad. Sci. USA 79:3033–36. With J. S. Lipsick, L. Serunian, and V. L. Sato. Differentiation and activation of nu/nu splenic T Cell precursors by mature peripheral T cells in the absence of thymus. J. Immunol. 129:40–45. 1983 With T. F. Bumol, Q. C. Wang, and R. A. Reisfeld. Monoclonal antibody and an antibody-toxin conjugate to a cell surface proteoglycan of melanoma cells suppress in vivo tumor growth. Proc. Natl. Acad. Sci. USA 80:529–33. With M. Goodman, M. S. Verlander, K. L. Melmon, K. A. Jacobson, A. B. Reitz, J. P. Taulane, and M. A. Avery. Characterization of catecholamine-polypeptide conjugates. Eur. Polym. J. 19:997–1004. 1984 With G. M. Beattie, J. F. Reece, and J. F. Villela. A leukemia virus-related protein in the murine pancreas. Biochem. Biophys. Res. Commun. 124:344–49.
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Biographical Memoirs: Volume 63 1985 With J. F. Leis and A. F. Knowles. Demonstration of separate phosphotyrosyl- and phosphoseryl-histone phosphatase activities in the plasma membranes of a human astrocytoma. Arch. Biochem. Biophys. 239:320–26.
Representative terms from entire chapter: