Click for next page ( 149


The National Academies | 500 Fifth St. N.W. | Washington, D.C. 20001
Copyright © National Academy of Sciences. All rights reserved.
Terms of Use and Privacy Statement



Below are the first 10 and last 10 pages of uncorrected machine-read text (when available) of this chapter, followed by the top 30 algorithmically extracted key phrases from the chapter as a whole.
Intended to provide our own search engines and external engines with highly rich, chapter-representative searchable text on the opening pages of each chapter. Because it is UNCORRECTED material, please consider the following text as a useful but insufficient proxy for the authoritative book pages.

Do not use for reproduction, copying, pasting, or reading; exclusively for search engines.

OCR for page 148

OCR for page 148
HERMAN MORITZ KALCKAR March 26, I908-May I 7, 199' BY EUGENE P. KENNEDY HERMAN MORITZ KAECKAR died in Cambridge, Massachu- setts, on May 17, 1991, at the age of eighty-three. His scientific career spanner! much of the perioc! of clevelop- ment of moclern biochemistry, to which he macle contribu- tions of central importance. Kalckar was born in Copenhagen on March 26, 190S, into a family he clescribec! in an autobiographical essay as having been micicIle-ciass Jewish-Danish for many genera- tions. Kalckar's broac! interests in literature en c! the arts hac! their origins in his early family life. His mother, Bertha Rosalie Melchior KaTckar, react wiclely in French en c! Ger- man as well as Danish literature. His father, Lucivig Kalckar, a businessman, was clevotec! to music en c! the theater. Lucivig KaTckar attenclec! the woric! premiere of Ibsen's "A Doll's House" at the Royal Theater in Copenhagen in November IS79 and later wrote an enthusiastic review of it. Herman KaTckar tracer! some of his own enthusiasm for music, en c! in particular for Mozart, to his father's example. Herman's younger brother, Fritz Kalckar, was a giftec! physicist en c! a colleague en c! protege of Niels Bohr. The death of Fritz in 1938 at twenty-eight years of age was a devastating blow for the entire family. 149

OCR for page 148
50 B I O G RA P H I C A L EMOIRS KaTckar receiver! his early schooling in the Ostre Borgerclyc! Skole, locater! within an easy walk of his home in Copenhagen. The headmaster, I. L. Heiberg, was a Greek scholar of inter- national repute, en c! KaTckar pair! tribute to the "Athenian flavor" of the school. He felt a special gratitude to the phys- ics teacher, H. C. Christianson, whom he recallec! many years later as a formiciable en c! passionately clevotec! teacher. Kalckar completec! his studies for a degree in medicine at the University of Copenhagen in 1933 en c! then began his scientific career in 1934 as a cancliciate for the Ph.D. degree in the Department of Physiology under the direc- tion of Ejnar LuncisgaarcI. Luncisgaarc! hac! earlier macle the important fincling that frog muscles poisoner! with iocloacetate en c! therefore unable to carry out glycolysis (the splitting of glucose to lactic acicI) are nevertheless capable of carrying out a limiter! number of contractions. Luncisgaarc! later shower! that these "nonIactic" contractions were at the expense of the clephosphorylation of creating phosphate, which hac! been cliscoverec! en c! characterizec! only a few years earlier by Cyrus Fiske at the Harvarc! Meclical School. In 1932 Fritz Lipmann, unable to work in Nazi Germany, mover! to Copenhagen, where he was closely associates! with LuncisgaarcI. Lipmann became one of Kalckar's mentors en c! a close friend, a relationship that was to be lifelong. Lipmann was already deeply interested not only in Lundsgaard's work on the role of phosphate esters in muscle contraction but also in the biological functions of phosphorylation reac- tions more generally. In his masterly and highly influential review in 1941 Lipmann was to emphasize the central role of aclenosine triphosphate (ATP) as an "energy-rich" phos- phate ester, the breakdown of which to aclenosine cliphos phate (ADP) and inorganic phosphate (Pi) drives not only muscle contraction but also a host of other energy-requir- ing processes. Because the cell has a limiter! supply of ATP,

OCR for page 148
HERMAN MORITZ KALCKAR 151 the ADP former! by its breakdown must be continuously rephosphorylatec! to AT P. In muscle this may be clone by use of creating phosphate, a cellular reserve of "energy-rich phosphate" that is present, however, only in limiter! amounts. At that time the only primary source of energy known to biochemists for the rephosphorylation of ADP to ATP was the splitting of glucose to lactic acid in muscle or in yeast to alcohol en c! carbon clioxicle. The brilliant achievements of Otto Warburg (which both Kalckar en c! Lipmann greatly acimirecI) hac! reveaTec! the reactions by which ADP is phos- phorylated to ATP during glycolysis. Glycolysis, however, is a process that can occur anaerobi- cally in the absence of molecular oxygen. Classic investiga- tions by Pasteur hac! macle it clear that aerobic metabolism of glucose by yeast is vastly more energy efficient than the anaerobic process. How is energy captures! by the oxicia- tion of sugars en c! other foodstuffs linker! to the recluction of molecular oxygen? This was the question confronted by KaTckar as he began the investigations in the period 1937 39 that lee! him to the demonstration that cell-free extracts of kiciney cortex catalyze oxiciative phosphorylation that is, the formation of ATP in reactions strictly clepenclent on the recluction of oxygen en c! inclepenclent of glycolysis. An important technical point in these experiments was the use of soclium fluoride to inhibit interfering phosphatases that otherwise wouIc! break clown ATP en c! other phosphate es- ters almost as soon as they were formed. As is now well known, aerobic nonphotosynthetic organ- isms, inclucling ourselves, derive vastly more metabolic en- ergy from oxiciative phosphorylation than from any other source. It is estimates! that the complete utilization of glu cose in muscle leacis to the procluction of about seventeen times more ATP via oxidative phosphorylation than is pro- duced in anaerobic glycolysis. Oxidative phosphorylation is

OCR for page 148
152 B I O G RA P H I C A L EMOIRS therefore a process of central bioenergetic importance. It became (anc! still is) the object of intensive studies in many laboratories throughout the worIcI. Localizec! in the inner membrane of the mitochoncirion, oxiciative phosphoryla- tion prover! extraorclinarily resistant to biochemical clissec- tion. Two clecacles were to pass before real insight was gainer! into the mechanism of oxiciative phosphorylation with the clevelopment by Peter Mitchell of the chemiosmotic theory. To this ciate many important features of oxiciative phos- phorylation remain imperfectly unclerstoocI, but KaTckar's work openec! the way to its systematic exploration. At about the same time as Kalckar's experiments V. A. Belitzer, working in virtual isolation in the Soviet Union, macle similar observations on oxiciative phosphorylation in experiments on preparations clerivec! from pigeon breast muscle. Although Belitzer's work clic! not become known in western Europe until a consiclerable time after Kalckar's first publications, it was characteristic of Kalckar that he was always generous in acknowleciging Belitzer's contribu- tion. During his trip to the Soviet Union in 1960 Kalckar looker! up Belitzer in Kiev en c! took some pains to make arrangements to be photographer! with him. Kalckar's early experiments on oxidative phosphorylation also provided evidence for the production of phospho- enolpyruvate from fumaric or maTic acids, observations that later proviclec! an important clue to the mechanisms in- volvec! in the formation of glucose from noncarbohycirate sources in animal tissues. Kalckar later wrote an interesting historical account of the origins of the concept of oxiciative phosphorylation en c! his early experimental work on this theme (1974~. In 1939, having completer! his work for the Ph.D. degree, Kalckar was appointed a Rockefeller research fellow for a year of postcloctoral stucly at the California Institute of Tech

OCR for page 148
HERMAN MORITZ KALCKAR 153 nology. On his trip across the Uniter! States he stopper! at the famous laboratory of Gerty en c! Car! Cori at Washing- ton University in St. Louis, then one of the few centers of the "new biochemistry" in the Uniter! States. There he fount! Siciney Colowick, then a graduate student, attempting to duplicate Kalckar's experiments on oxidative phosphoryla- tion, without success. Colowick, untrainec! in the methods introclucec! by Warburg en c! follower! by Kalckar, hac! been simply incubating tissue extracts in test tubes without pro- vicling for the efficient diffusion of oxygen into them. Thirty- five years later Colowick summarizer! Kalckar's helpful acI- vice: "'Shake it!' sail! Dr. K., en c! everything was OK!" KaTckar's stay in California allowed! him to take the fa- mous microbiology course in Pacific Grove taught by C. B. van Niel, whose insight into the unclerlying unity of the biochemistry of living organisms en c! charismatic personal- ity macle a creep impression on Kalckar, as on so many oth- ers. This experience may have planter! a seer! that lee! later to KaTckar's interest in microbial molecular biology. During his stay in Pasadena, with the encouragement of Linus Pauling, Kalckar undertook the preparation of a com- prehensive review of bioenergetics with emphasis on the role of phosphate esters in energy transduction. Its publica- tion (1941) clic! much to advance the new icleas that he en c! ~ L~pmann were pursuing. In ~ 940 Kalckar acceptec! an appointment as research fellow in Cori's Department of Pharmacology at Washing- ton University. The invasion of Denmark by the Nazis in the spring of 1940 hac! macle it impossible for Kalckar en c! his wife, Vibeke, to return to Copenhagen, en c! Kalckar was fortunate to have the opportunity to spenc! the next three years in a stimulating en c! productive environment with con- genial colleagues. He joiner! forces with Siciney Colowick. Their work lee! them to the discovery in muscle extracts of

OCR for page 148
54 B I O G RA P H I C A L EMOIRS a remarkable enzyme, namer! myokinase by them, but now more precisely caller! aclenylate kinase, that catalyzes the following reaclily reversible reaction: ATP + AMP 2 ADP (~y Many biological processes leac! to the production of acI- enosine monophosphate (AMP), which, however, cannot be phosphorylated to ATP during oxidative phosphorylation or glycolysis, processes that are specific for ADP as phos- phate acceptor. In the absence of reaction all, which "res- cues" AMP by converting it to ADP, all of the aclenine nucle- oticles of the cell wouic! be irreversibly converter! to AMP. Later experiments by other workers shower! that mutations that block the activity of aclenylate kinase are lethal to cells of Escherichia coli. In 1943 Kalckar was appointee! research associate at the Public Health Institute of the city of New York. One of the attractions of the post was a laboratory equipped with a new ultraviolet spectrophotometer, then still a rather rare instrument. Kalckar clevelopec! spectrophotometric meth- ocis for the stucly of the metabolism of nucleosicles en c! nucleoticles, the builcling blocks of RNA en c! DNA. It hac! earlier been reporter! by Klein that the enzymic hycirolysis of nucleosicles is stimulates! by the aciclition of phosphate or arsenate. Coming from the Cori laboratory, the center of work on glycogen phosphorylase, Kalckar realized the possible significance of the role of phosphate en c! soon macle the important discovery that the phosphorolytic cleav- age of nucleosides is similar to that of glycogen. r~oose-hypoxanth~ne + Pi . . . ribose-~-P + hypoxanthine (2)

OCR for page 148
HERMAN MORITZ KALCKAR 155 The reaction is reacliTy reversible. IncleecI, the equilibrium position lies to the left of Equation (2) as written, favoring the synthesis of the nucleosicle rather than its breakdown. As the first demonstration of the enzymic synthesis of a nucleosicle, this work attracted! consiclerable attention. It must be recalled! that in 1945, when this work was clone, very little was known of the metabolism of nucleic acids or incleec! of their functions in living cells. Later work was to show that nucleosicle phosphorylases function as "salvage enzymes" in the clegraciation rather than the synthesis of builcling blocks of nucleic acid. In 1946 Kalckar returned to Copenhagen, where a new laboratory was set up for him with the support of Ejnar Luncisgaarc! en c! with financial backing from American as well as Danish sources. The principal theme of research at the new "Cytofysiologisk Institute" was the metabolism of nucleosides and nucleotides. Kalckar attracted gifted young collaborators, such as Hans Klenow, Morris Friec~kin, en c! Walter McNutt, en c! the laboratory became a leacling center for work in this fielcI. In 1952 Kalckar began his studies on the metabolism of galactose in microbial en c! animal tissues. This became a principal pursuit after his move to the National Institutes of Health in 1952, first as a visiting scientist en c! later with a permanent appointment at the National Institute of Arthri- tis en c! Metabolic Diseases. In mammals the utilization of galactose, a component of milk sugar en c! therefore a major constituent in the cliet of infants, begins with its phosphorylation to galactose-~-P, which then must be converted to glucose-~-P, the further metabo- lism of which occurs by well-known reactions. The pioneer- ing work of Luis Leloir lee! to the discovery of the central role of uricline cliphosphate derivatives in the interconversion of galactose en c! glucose, sugars that are epimers, that is,

OCR for page 148
56 BIOGRAPHICAL MEMOIRS differing in configuration only at a single carbon atom (C- 4~. Leloir shower! that the two sugars are interconvertec! in the form of their uricline cliphosphate derivatives as in Equa- tion (4), catalyzer! by an epimerase, en c! suggester! that the synthesis of uridine diphosphate galactose (galactose-~-P-P- uricline~ might take place by reaction ~3): galactose-~-P + glucose-~-P-P-uridine ~alactose-~-P-P-uricline + ~lucose-~-P (3) a a NAD galactose-~-P-P-uridine glucose-~-P-P-uridine (4) In the sum of (3) en c! (4) the uricline-linkoc! forms of the sugars cancel out, en c! the overall reaction is: galactose-~-P glucose-~-P (3 + 4) In 1953 Kalckar en c! his collaborators reporter! direct evi- dence that the synthesis of uridine diphosphate galactose floes in fact occur in extracts of the yeast Saccharomyces Francis by reaction (3), catalyzed by the enzyme galactose-~-P uridyly! transferase. They also fount! an alternative reaction for the synthesis of uricline cliphosphate galactose in yeast: galactose-~-P + P-P-P-uridine galactose-~-P-P-uridine + P-P (5) It is important to note that reaction (5) floes not occur in human tissues, in which reaction (3), catalyzed by the uridyly! transferase, is an essential step in the utilization of galac- tose as an energy source. KaTckar clevisec! a methoc! to determine the levels of the

OCR for page 148
HERMAN MORITZ KALCKAR 157 uriclyly! transferase catalyzing reaction (3) in Tysates of rec! blooc! cells, employing his favorite spectrophotometric ap- proach. At just this time Kurt Isselbacher was also at NIH, carrying out research in collaboration with Gordon Tomkins en c! Julius AxeIrocI. As part of his clinical duties, Isselbacher was treating a chilc! whom he cliagnosec! as suffering from galactosemia, a severe inheritec! clisorcler characterizec! by the inability to break down galactose, which leads to accu- mulation of high levels of galactose in blooc! en c! tissues. Isselbacher sought out KaTckar, en c! a collaboration was be- gun that soon lee! to the fincling that the enzyme defect in the most serious form of human galactosemia is in the uriclyly! transferase that catalyzes reaction (3~. This in turn lee! to the clevelopment of a simple test for the presence or ab- sence of this enzyme in rec! blooc! cells that is now wiclely user! to screen newborn infants for galactosemia, a disease that can be effectively treater! by removal of milk en c! other sources of galactose from the cliet. The clevelopment of this test was of great practical consequence since early diagnosis is vital to prevent severe mental retardation en c! other cle- velopmental defects. In 1958 KaTckar acceptec! a professorship in the Depart- ment of Biology of Johns Hopkins University. This year also market! the publication of his highly original proposal that the contamination of foodstuffs from the fallout following atmospheric tests of nuclear weapons conic! be measurer! by the analysis of the content of strontium-90 in the milk- teeth of young chiTciren. As he pointer! out, measurement of racliation from clecicluous incisor teeth wouIc! reveal the levels of isotope ingestec! about seven years previous to shecI- cling of the teeth, when the caTcifiec! structure of the teeth had been deposited. By this proposal Kalckar hoped to fo- cus attention in a dramatic way on the pollution of the environment by tests of nuclear weapons. The iclea attracted!

OCR for page 148
58 B I O G RA P H I C A L EMOIRS consiclerable attention, en c! extensive collections of milk- teeth were in fact macle, particularly by a group of researchers at Washington University in St. Louis. It was learner! that milk-teeth from chiTciren born in 1956 container! about ten times more strontium-90 than teeth from chilciren born in 1950. Fortunately, after the ban on atmospheric testing the levels fell once again to Tower levels. In 1961 Kalckar mover! to the Harvarc! Meclical School as professor of biological chemistry ant! heat! of the Biochemical Research Laboratory of Massachusetts General Hospital (MGH). He succeeclec! Fritz Lipmann in that position. Here he continues! his studies on the metabolism of galactose in animal tissues with special attention to the epimerase that catalyzes reaction (4) above. Kalckar now also became cleeply interested! in the role of the cell surface in sensory processes en c! in cell signaling en c! often referrer! to this fielcI, then newly emerging, as "ektobiology." Winfriec! Boos, his young colleague at MGH, carrier! out an intensive stucly of the transport of galactose into cells of E. coil, which culminates! in the isolation en c! cletailec! characterization of a specific galactose-bincling pro- tein that was shown to be an essential part of the transport system. Julius Adler and his colleagues at the University of Wisconsin cliscoverec! at about the same time that cells of E. cold can detect the presence of galactose in the meclium en c! "chase" this sugar by a positive chemotactic response. Kalckar immecliately suggester! that the galactose-bincling protein that could "recognize" galactose for transport might also be needler! for the chemotactic response. The first tests of this notion, however, were clisappointingly negative. Kalckar per- sistec! in his iclea, however, ant! further experiments reveaTec! that an unexpected complexity of the transport system had renclerec! the first tests invalicI. The final definitive experi- ments reveaTec! that the bincling protein plays a vital role

OCR for page 148
HERMAN MORITZ KALCKAR 159 not only in the transport of galactose but also in chemot- axis, an outcome that gave Kalckar consiclerable satisfac- tion. KaTckar was also greatly interested! in the conversion of galactose to cell-surface lipopolysaccharicles in bacteria, work vigorously pursues! in his MGH laboratories by Hiroshi Nikaiclo. Nikaiclo's pioneering studies on the biosynthesis of lipopolysaccharide in Salmonella employed both genetic en c! biochemical approaches en c! clic! much to clarify the complex reaction sequences, particularly the role of lipicI- linkoc! intermediates. Kalckar turner! next to the problem of the regulation of the transport of sugars into mammalian cells en c! the im- portance of this process in tumor cells. This work was in part stimulates! by a collaborative study in 1973 with Sen- itiroh Hakomori at the University of Washington in Seattle on carbohydrate utilization en c! the uptake of galactose in hamster cells transformer! by polyoma virus. In 1974 KaTckar retiree! as heat! of the Biochemical Re- search Laboratory but continues! his research as visiting professor in the Huntington Laboratories at MGH until 1979. At that time he mover! to the Department of Chemistry at Boston University as clistinguishec! research professor, an appointment he greatly valued because it permitted him to continue his research interests in a new en c! stimulating environment to the very ens! of his life. The work on hex- ose transport en c! metabolism in normal en c! malignant cells continued to be the theme of much of the work in the laboratory at Boston University en c! the subject of many papers with his longtime collaborator, Donna Ullrey, the last of which was publisher! only shortly before his cleath. Kalckar's achievements in science brought him wicle rec- ognition, inclucling election to the National Academy of Sciences, the Royal Danish Academy, and the American Acad

OCR for page 148
60 B I O G RA P H I C A L EMOIRS emy of Arts en c! Sciences, as well as honorary degrees from Washington University, the University of Chicago, en c! the University of Copenhagen. To his many friends, KaTckar's character en c! personality were as impressive as his scientific accomplishments. Through- out his entire career Kalckar won the affection en c! acimira- tion of a large number of students en c! junior associates who were trainee! in his laboratory. The sweep of his intel- lect was very broacI, his spirit was open en c! generous, en c! he hac! a wonclerfuT sense of humor. Upon first acquain- tance many fount! it clifficult to follow the threat! of his discourse, partly because he was apt to begin a new topic in medics res without explanatory preamble en c! partly because he often pair! the listener the compliment of omitting from a chain of reasoning the links that seemec! obvious. After one became accustomec! to this style it enhancer! the effect of his gentle, unclerstatec! wit. The same enlightenec! humanism that shaper! Kalckar's tastes in music en c! the arts was evident in his view of woric! problems, as eviclencec! by his concern for the mounting threat of nuclear warfare en c! the ciangers of continues! testing of nuclear weapons, which he hac! ciramatizec! by the milk-teeth collection project. Kalckar's first marriage, to the musician Vibeke Meyer, enclec! in divorce in 1950. Three chiTciren, Sonja, Nina, en c! Niels, to whom he was cleeply clevotecI, were born of his second marriage to the developmental biologist Barbara Wright. After clissolution of that marriage, KaTckar in 1968 marries! the interior designer Agnete Friclericia Laursen, who survives him. For the last twenty-three years of his life, Agnete's love and support were an essential part of Herman's life, en c! their home in Cambridge was a focus of warmth en c! hospitality for friends en c! colleagues.

OCR for page 148
HERMAN MORITZ KALCKAR SELECTED BIBLIOGRAPHY 1937 Phosphorylation in kidney tissues. Enzymologia 2:47. 1938 161 Formation of a new phosphate ester in kidney extracts. Nature 142:871. 1939 Coupling between phosphorylations and oxidations in kidney ex- tracts. Biochem. f. 6:209. 1941 The nature of energetic coupling in biological synthesis. Chem. Rev. 28:71. With S. P. Colowick. An activator of the hexokinase system. 7. Biol. Chem. 137:789. 1942 The enzymatic action of myokinase. 7. Biol. Chem. 143:299. 1943 With S. P. Colowick. The role of myokinase in transphosphorylations. I. The enzymatic phosphorylation of hexoses by adenylpyrophosphate. f. Biol. Chem. 148: 117. 1944 Spectroscopic microdetermination of muscle adenylic acid. Science 99:131. 1945 Enzymatic synthesis of a nucleoside. 7. Biol. Chem. 158:723. 1947 The enzymatic synthesis of purine ribosides. 7. Biol. Chem. 167:477.

OCR for page 148
162 B I O G RA P H I C A L 1948 EMOIRS With H. Klenow. Enzymatic transformation of pteroylglutamic acid. f. Biol. Chem. 172:351. 1949 With M. Friedkin and E. Hoff-Jorgensen. Enzymatic synthesis of desoxyribose nucleoside with desoxyribose phosphate ester. 7. Biol. Chem. 178:527. 1952 Enzymatic reactions in purine metabolism. Harvey Lect. Ser. 45, pp. 11-39. 1953 With B. Braganea and A. Munch-Petersen. Uridyl transferases and the formation of UDP-galactose. Nature 172:1038. 1954 Biosynthesis and metabolism of phosphorus compounds. Annul Rev. Biochem. 23:527. With J. L. Strominger, J. Axelrod, and E. Maxwell. Enzymatic oxida- tion of uridine diphosphate glucose to uridine diphosphate glu- curonic acid. J. Am. Chem. Soc. 76:6411. 1955 With E. Maxwell and R. M. Burton. Galacto-waldenase and the enzy- matic incorporation of galactose-l-phosphate in mammalian tis- sues. Biochim. Biophys. Acta 18:389. 1956 With E. P. Anderson and K. J. Isselbacher. Galactosemia, a congeni- tal defect in a nucleotide transferase. A preliminary report. Proc. Natl. A cad . Sci. U. S. A. 42:49. With K. J. Isselbacher, E. P. Anderson, and K. Kurahashi. Congeni- tal galactosemia, a single enzymatic block in galactose metabo- lism. Science 123:635. 1957 Biochemical mutations in man and microorganisms. Science 125:105.

OCR for page 148
HERMAN MORITZ KALCKAR 163 With E. P. Anderson, K. Kurahashi, and K. T. Isselbacher. A specific enzymatic assay for the diagnosis of congenital galactosemia. I. The consumption test. 7. Lab. Clin. Med. 50:469. 1958 An international milk teeth radiation census. Nature 182:283. With E. Maxwell and H. de Robichon-Szulmajster. Yeast uridine diphosphate galactose-4-epimerase: correlation between activity and fluorescence. Arch. Biochem. Biophys. 78:407. 1962 With T. A. Sundararajan and A. M. C. Rapin. Biochemical observa- tions on E. cold mutants defective in uridine diphospho-glucose. Proc. Natl. Acad. Sci. U.S.A. 48:2187. 1965 Galactose metabolism and cell sociology. Science 150:305. 1968 With A. M. C. Rapin and L. Alberico. The metabolic basis for mak- ing of receptor sites on E. Coli K12 for C21, a lipopolysaccharide core-specific phage. Arch. Biochem. 128:95. 1969 Biological Phosphorylations: Development of Concepts. Englewood Cliffs, N.T.: Prentice-Hall. With H. C. P. Wu and W. Boos. Role of the galactose transport system in the retention of intracellular galactose in Escherichia coli. J. Mol. Biol. 41:109. 1971 The periplasmic galactose binding protein of Escherichia coli. Science 174:557. 1973 With D. Ullrey, S. Kijomoto, and S. Hakomori. Carbohydrate ca- tabolism and the enhancement of the uptake of galactose in hamster cells transformed by polyoma virus. Proc. Natl. A cad. Sci. U.S.A. 70:839.

OCR for page 148
164 B I O G RA P H I C A L 1974 EMOIRS Origins of the concept of oxidative phosphorylation. Mol. Cell. Biochem. 5 55 ~ 1975 With T. J. Silhavy and W. Boos. The role of the Escherichia cold galac- tose-binding protein in galactose transport and chemotaxis. In Twenty-fifth Mosbacher Colloquium, ed. L. Jacnicke, pp. 1-30. Ber- lin: Springer-Verlag. 1976 Cellular regulation of transport and uptake of nutrients: an over- view. 7. Cell. Physiol. 89:503 1985 With P. Plesner and D. B. Ullrey. Mutations in the phosphoglucose isomerase gene can lead to marked alterations in cellular ATP levels in cultured fibroblasts exposed to simple nutrient shifts. Proc. Natl. Acad. Sci. U.S.A. 82:2761. 1986 Autobiographical notes from a nomadic biochemist. In Selected Top- ics in the History of Biochemistry, ed. G. Semenza and R. Jacnicke, pp. 101-76. Amsterdam: Elsevier Science Publishers. 1991 Fifty years of biological research from oxidative phosphorylation to energy-requiring transport regulation. Annul Rev. Biochem. 60:1. With D. B. Ullrey. Search for cellular phosphorylation products of D-allose. Proc. Natl. Acad. Sci. U.S.A. 88:1504.

OCR for page 148