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Biographical Memoirs: Volume 61 CARL FERDINAND CORI December 5, 1896-October 19, 1984 BY MILDRED COHN UNRAVELING THE glycolytic and glycogenolytic pathways was a remarkable feat and a testament to the imagination and ingenuity of all those who participated. Carl and Gerty Cori contributed an essential part and in so doing were among the pioneers who showed that biochemical investigations of isolated enzyme systems could lead to an understanding of physiological processes. From their discovery of the first product of glycogen breakdown, glucose-1-phosphate, the Coris went on to isolate and crystallize the enzyme phosphorylase that catalyzed the reaction—the first of a class of reactions in which inorganic orthophosphate reacts to yield an organic phosphate ester. Glycogen phosphorylase proved a treasure trove for biochemistry. By reversal of the phosphorylase reaction, it was shown that a macromolecule could be synthesized in a cell-free system. The enzyme was further found to exist in two interconvertible forms, though one was inactive in the absence of adenylic acid, which acted as an effector. The next generation of scientists trained in the Cori laboratory, using the Coris' fundamental discoveries, probed still further and discovered the two most widespread metabolic regulatory mechanisms: the cyclic AMP system and phos-

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Biographical Memoirs: Volume 61 phorylation-dephosphorylation of enzymes accompanied by a cascade system of control. EUROPE (1896-1922) Carl Cori never regretted leaving Europe at the age of twenty-five to come to the United States and grew to be thoroughly at ease with the language, institutions, and customs of his chosen country. Yet he was, and would always be, a product of his cultured European background. Carl Ferdinand Cori was born in Prague (then part of the Austro-Hungarian empire) on October 19, 1984. When he was two the family moved to Trieste, where his father took over as director of the Marine Biological Station. Carl spent his formative early years in Trieste, and his autobiographical essay, ''The Call of Science'' (1969), paints the picture of a happy childhood in a cultured and international milieu. In Trieste, Carl came into contact with a variety of ethnic groups. He was soon fluent in Italian, and the racial tolerance he developed there proved to be life long. Educated at the classical gymnasium from 1906 to 1914, furthermore, he obtained a grounding in Latin and Greek he would never forget. Just as important, however, was the informal education he received at the Marine Biological Station. During field trips on the motorboat "Adria," his father, who captained the boat, lectured on the geology, botany, and early cultural history of the coastal region in addition to its oceanography and marine biology. Renowned for his own broad erudition in biology, archaeology, and history, the younger Cori attributed his abiding interest in them to his experiences on these field trips. Summers with his extended family in the Austrian Tyrol rounded off Carl's education by giving him a love of mountaineering and music. His only rebellion, he records, was

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Biographical Memoirs: Volume 61 a certain penchant for practical jokes aimed at embarrassing his parents. His reference to a crystal of permanganate in the chamber pot, for example, caused consternation for a visiting maiden aunt with hypochondriac tendencies. Carl's family boasted illustrious scientists and academics on both sides. Ferdinand Lippich, his maternal grandfather and professor of mathematical physics at the German University of Prague, had (in addition to making theoretical contributions to physics) developed the polarimeter as a precision instrument. Wilhelm Lippich, his great-grandfather, had been an anatomist at the University of Padua and a professor in Vienna. His uncle Friedrich Lippich was professor of chemistry in Prague, while his father, Carl I. Cori, was one of Europe's leading zoologists and marine biologists. Prominent scientists, furthermore, were frequent visitors to the house, and it is hardly surprising that young Carl chose to embark on a scientific career. In 1914, at the age of seventeen, he entered the Carl Ferdinand University (the German university of Prague) to study medicine—at that time the customary route to a research career in the life sciences. He was fortunate to find there an intelligent and charming fellow student, Gerty Radnitz, who shared his interest in science and love of the outdoors. In 1916, while still medical students, they published their first joint research paper. Later, Gerty became Carl's wife and was, until her death in 1957, his dedicated scientific collaborator. During World War I, in his third year at the university, Carl was drafted into the Austrian army. He was first stationed in a bacteriology laboratory, where—after a severe bout of typhoid fever he ascribed to his own carelessness—he taught himself a meticulous technique for handling pathogens. Later he served in a hospital for infectious diseases near the Italian front. Because of his knowledge of Italian,

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Biographical Memoirs: Volume 61 he was charged with caring for civilians as well as soldiers. While he could help some patients with the drugs then available, he found tuberculosis, malaria, pellagra, scurvy, and typhoid rampant in this poorly nourished population. His inability to help the victims of an influenza epidemic shocked him. This, along with the experience of a long and dangerous retreat amid a mass of undisciplined soldiers, made him skeptical about the practice of medicine and strongly averse to war ever after. Cori returned to Prague in 1918, completed his clinical studies, and was awarded the M.D. degree. He and Gerty were married in Vienna, where both had gone to do postdoctoral work, in August 1920. He divided his laboratory work between the university's Pharmacology Institute and its internal medicine clinic but found his experiences in the latter so discouraging that he had no desire to continue in clinical medicine. The alternative—a career devoted entirely to research—was attractive both to him and to Gerty. Unfortunately, the postwar devastation in Austria made it highly unlikely that they would find paid positions; one could hardly get enough to eat. Gerty Cori, working at Karolinen Children's Hospital, developed symptoms of xerophthalmia from the inadequate diet provided for her there. Fortunately, Carl Cori's research on the mechanism of seasonal variation of vagus action in the frog heart (1921) caught the attention of H. H. Meyer, who had just retired from the Pharmacology Institute. In the summer of 1921, Dr. Gaylord, director of the State Institute for the Study of Malignant Diseases (now the Roswell Park Memorial Institute) in Buffalo, New York, asked Meyer to suggest a biochemist for his institution. Meyer recommended Cori, who was interviewed for the position but was so certain that nothing would come of it that he accepted a position with

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Biographical Memoirs: Volume 61 Otto Loewi in the Pharmacology Department of the University of Graz. Cori stayed at Graz only six months, during which he learned a great deal. Loewi's enthusiasm and originality coupled with his wide knowledge of all aspects of biomedical science made him an invaluable mentor. It was during this intellectually stimulating period that Cori first thought of a way to study intestinal absorption, and the fate of sugar, in general, in the animal body. But other aspects of the Graz experience were decidedly unpleasant. To be eligible for employment at the university, Cori had had to prove his Aryan descent, and despite his scientific stature, Otto Loewi's future there was questionable. Living conditions and research facilities were woefully inadequate. When Gaylord offered Cori the position in Buffalo, therefore, both he and Gerty Cori welcomed the opportunity to leave Europe. Carl left early in 1922, and Gerty joined him six months later. BUFFALO, NEW YORK (1922-31): STATE INSTITUTE FOR THE STUDY OF MALIGNANT DISEASES-ROSWELL PARK MEMORIAL INSTITUTE In Buffalo, Cori initiated his life's work on carbohydrate metabolism and its regulation. Obliged to do routine laboratory tests for the hospital affiliated with the Institute, he used the opportunity to hone his analytical skills. His first paper on carbohydrate metabolism was published in 1922; in the ensuing decade, he published some eighty papers. After some initial problems in 1922-23 (1969,1), Gerty Cori, who had a position in the Institute's pathology department, was allowed to collaborate with Carl, and the majority of those eighty papers are joint publications. In the following discussion no attempt will be made to assess individual contributions because it was the work of two peers speak-

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Biographical Memoirs: Volume 61 ing with one inseparable voice. As Carl Cori stated (1947,1): "Our efforts have been largely complementary; and one without the other would not have gone so far as in combination." Regulation of Glucose Concentration in the Blood The question the Coris wanted to answer was: What regulates blood glucose concentration? Their initial experiments were physiological, designed to determine the amount of sugar absorbed in the alimentary tract by measuring the unabsorbed sugar left in the gut of a rat after it had ingested a known amount (1925,5). This was followed by experiments with a new method devised to determine the glycogen content of liver and carcass separately. But in order to assess changes in glycogen concentration after sugar ingestion or hormone administration, a control value had first to be established. It was found that the glycogen concentration was fairly constant in rats fasting for twenty-four to forty-eight hours. Higher and more uniform glycogen concentrations, furthermore, could be obtained by giving an amount of glucose that could be absorbed completely in three hours. Having established conditions and analytical methods that were reproducible, it was then possible to do balance studies to determine the fate of the absorbed glucose in fasted rats and the influence insulin and epinephrine had on that fate. The researchers found that insulin increased oxidation of glucose and conversion to muscle glycogen but decreased conversion to liver glycogen (1926,1, 1928,1). Epinephrine, on the other hand, decreased muscle glycogen and increased liver glycogen (1928,2,3). Since it was known that muscle glycogen does not contribute glucose to blood, the Coris concluded that another intermediate must be formed from muscle glycogen and circulated through

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Biographical Memoirs: Volume 61 the blood to the liver to become the precursor of liver glycogen. Since it was known that lactic acid was formed when glycogen disappeared in muscle, the Coris postulated—and later demonstrated—that lactate was the intermediate in the "cycle of carbohydrates" (1928,2,3). The "cycle of carbohydrates," which the researchers represented in the diagram given below (1929,1): came to be known as the "Cori cycle." This scheme derived from research on the circulation of carbohydrate material in the intact animal was a milestone in the elucidation of carbohydrate metabolism and, along with other insights on blood homeostasis, helped clarify the action of epinephrine on blood glucose. Yet equally important were the reliable—and reproducible—techniques developed by the Coris to detect and quantify even small changes in liver glycogen, on which their research depended. Influential Publications During his stay at the Institute in Buffalo, Carl Cori also published a number of papers dealing with cancer. In 1923, Otto Warburg found that tumors display higher aerobic and anaerobic glycolysis than normal tissue. But Warburg's studies were carried out in vitro, and the Coris were the first to demonstrate that tumors in intact animals also showed abnormally high formation of lactic acid from glucose (1925,4). In 1931, Cori wrote a masterly review on mammalian carbohydrate metabolism (1931,4). With more than 100

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Biographical Memoirs: Volume 61 pages and some 500 cited references, the review included a critical evaluation of the literature, a summary of the pioneering work Carl and Gerty Cori had accomplished, and an indication of the direction of their future research on the mechanism of glycogenolysis. It established Carl Cori as a leader in the field and influenced the study of carbohydrate metabolism for many years to come. WASHINGTON UNIVERSITY SCHOOL OF MEDICINE, ST. LOUIS (1931-45) In 1931, Carl and Gerty Cori moved to St. Louis, where Carl became the chairman of the Pharmacology Department at Washington University and Gerty was given a position in the department, albeit with a token salary. In addition to his research, however, Cori was now expected to organize a department, equip a research laboratory, and spend considerable time teaching medical students. Understandably, there was a hiatus in the publication of papers. During the last phase of the Buffalo period, however, the Coris had started working with isolated muscle preparations rather than intact animals. From balance-studies with epinephrine, they had concluded that the formation of a precursor of lactate from glycogen that accumulates in muscle is accompanied by the disappearance of inorganic phosphate (1930,5). They had developed a method, furthermore, for detecting hexose monophosphate simultaneously as both hexose and phosphate (1931,3). These experiments were a prelude to their important discovery of glucose-1-phosphate, for it was in St. Louis that their research progressed in the direction of biochemistry. Phosphorylase—The Cori Ester To study the concomitant disappearance of glycogen and phosphate, the Coris decided to use minced skeletal muscle

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Biographical Memoirs: Volume 61 from frogs. When the water extracted, muscle dispersions were incubated anaerobically in phosphate buffer, and they observed that—unless boiled muscle extract were added—only small amounts of hexose monophosphate were produced. In the first striking result from these experiments, they identified 5'-adenylic acid as an obligatory activator of the reaction (1936,4; 1938,1)—a finding that foreshadowed the idea that the allosteric activation of appropriate enzymes regulates metabolic processes. At the 1935 International Physiological Congress in Moscow, the Coris presented their results on the formation of hexose monophosphate from the reaction of glycogen with stoichiometric amounts of phosphate in rat and frog muscle. Subsequently investigating the reaction in muscle extracts on his own, J. K. Parnas confirmed that, simultaneous with the cleavage of glycogen, phosphate disappears—a reaction he characterized with the term "phosphorolysis." Because there was a large discrepancy in their analytical results for hexose monophosphate between phosphate- and reducing-power determinations, the Coris postulated the formation of a hitherto unknown phosphorylated, nonreducing precursor of hexose-6-phosphate. Having isolated this product as a crystalline brucine salt, they tentatively assigned it the structure of glucose-1-phosphate. They adduced, together with S. P. Colowick, final proof of this structure by synthesizing α-glucose-1-phosphate (1937,2), and it subsequently came to be known as the "Cori ester." Discovery of the Cori ester bore the hallmark of the Coris' meticulous approach to scientific problems. Their success depended first and foremost on reliable methods of analysis whose results could be quantified —as seen in their analysis of phosphorylated hexose. They took particular care, furthermore, with the design of their experiments—as exemplified by the series that led to their identification of the

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Biographical Memoirs: Volume 61 activator 5-AMP. Add to this the element of luck, for the muscle dispersions the Coris' chose as a medium allowed glucose-1-phosphate to accumulate. In intact muscle, the presence of Mg2+ causes the enzyme phosphoglucomutase (1938,3) to convert glucose-1-phosphate to glucose-6-phosphate, so that its concentration is nineteen times that of glucose-1-phosphate at equilibrium. But happily for the Cori experiments, in their method of muscle preparation, much of the Mg 2+ was "washed out." They suggested that, contrary to earlier notions, blood glucose in the liver is regulated by the sequential action of three enzymes: glycogen phosphorylase, phosphoglucomutase, and glucose-6-phosphatase—a sequence confirmed by their later work (1939,1). The Coris named their new-found enzyme, which catalyzed the formation of glucose-1-phosphate from glycogen and inorganic phosphate, "phosphorylase," consistent with Parnas's term "phosphorolysis" for the reaction. This new intermediate in glycogenolysis, furthermore, was novel in two ways. First, it was the first known example of the esterification with inorganic orthophosphate at the reducing group of a hexose. It was also evidence of a phosphorolytic cleavage of glycogen by the enzyme. Their 1936 discovery launched the Coris full-fledged into enzymology. Seeking to synthesize glycogen, they reversed the phosphorylase reaction, adding a small amount of glycogen when they observed a lag in its production (1939,3). This established the need of a primer in polysaccharide synthesis and produced as a product a large, starch-like polysaccharide (1940,2). For the first time, researchers working with a cell-free preparation had synthesized a macromolecule—an exciting demonstration that contradicted the long-held notion that the biosynthesis of macromolecules required energy-metabolism and could, therefore, occur only in intact cells.1

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Biographical Memoirs: Volume 61 SELECTED BIBLIOGRAPHY 1920 Zur Physiologie und Pharmakologie der Reizerzeugung am Herzen. Pfluegers Archiv. 184:272. With G. Radnitz. Über den Gehalt des menschlichen Blutserums an Komplement und Normalambozeptor für Hammelblutkörperchen. Z. Immunitaetsforsch. 29:445. 1921 Untersuchungen über die Ursachen der Unterschiede in der Herznervenerregbarkeit bei Fröschen zu verschiedenen Jahreszeiten. Ein Beitrag zur Frage des peripheren Antagonismus von Vagus und Sympathikus und zur Beeinflussung der Herznerven durch Schilddrüsensubstanzen Arch. Exp. Pathol. Pharmakol. 91:130. 1923 With G. T. Cori and G. W. Pucher. The free sugar content of the liver and its relation to glycogen synthesis and glycogenolysis. J. Pharmacol. Exp. Ther. 21:377. With G. T. Cori and H. L. Goltz. Comparative study of the blood sugar concentration in the liver vein, the leg artery and the leg vein during insulin action. J. Pharmacol. Exp. Ther. 22:355. With G. W. Pucher and G. T. Cori. The free sugar in the liver and its significance for carbohydrate metabolism. Proc. Soc. Exp. Biol. Med. 20:522. With G. W. Pucher and G. T. Cori. The determination of galactose in the presence of glucose. Proc. Soc. Exp. Biol. Med. 20:523. With G. W. Pucher and B. D. Bowen. Comparative study of the blood sugar concentration in the arterial and venous blood of diabetic patients during insulin action. Proc. Soc. Exp. Biol. Med. 21:122. 1925 With G. T. Cori. Comparative study of the sugar concentration in arterial and venous blood during insulin action. Am. J. Physiol. 71:688. With H. L. Goltz. The influence of insulin on the inorganic and organic phosphates of the liver. Am. J. Physiol. 72:256. The influence of insulin and epinephrine on the lactic acid content of blood and tissues. J. Biol. Chem. 63:253.

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Biographical Memoirs: Volume 61 With G. T. Cori. The carbohydrate metabolism of tumors. II. Changes in the sugar, lactic acid, and CO2-combining power of blood passing through a tumor. J. Biol. Chem. 65:397. The fate of sugar in the animal body. I. The rate of absorption of hexoses and pentoses from the intestinal tract. J. Biol. Chem. 66:691. Insulin and liver glycogen. J. Pharmacol. Exp. Ther. 25:1. 1926 With G. T. Cori. The fate of sugar in the animal body. III. The rate of glycogen formation in the liver of normal and insulinized rats during the absorption of glucose, fructose, and galactose J. Biol. Chem. 70:577. 1927 The fate of sugar in the animal body. IV. The tolerance of normal and insulinized rats for intravenously injected glucose and fructose. J. Biol. Chem. 72:597. With G. T. Cori. The fate of sugar in the animal body. V. A seasonal occurrence of ketonuria in fasting rats accompanied by changes in carbohydrate metabolism. J. Biol. Chem. 72:615. With G. T. Cori. The fate of sugar in the animal body. VI. Sugar oxidation and glycogen formation in normal and insulinized rats during the absorption of fructose. J. Biol. Chem. 73:555. With G. T. Cori. The fate of sugar in the animal body. VII. The carbohydrate metabolism of adrenalectomized rats and mice. J. Biol. Chem. 74:473. 1928 With G. T. Cori. The fate of sugar in the animal body. VIII. The influence of insulin on the utilization of glucose, fructose, and dihydroxyacetone. J. Biol. Chem. 76:755. With G. T. Cori. The mechanism of epinephrine action. I. The influence of epinephrine on the carbohydrate metabolism of fasting rats, with a note on new formation of carbohydrates. J. Biol. Chem. 79:309. With G. T. Cori. The mechanism of epinephrine action. II. The influence of epinephrine and insulin on the carbohydrate metabolism of rats in the postabsorptive state. J. Biol. Chem. 79:321. With G. T. Cori. The carbohydrate metabolism of tumors. III. The rate of glycolysis of tumor tissue in the living animal. J. Cancer Res. 12:301.

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Biographical Memoirs: Volume 61 1929 With G. T. Cori. Glycogen formation in the liver from d- and l-lactic acid. J. Biol. Chem. 81:389. With G. T. Cori. The mechanism of epinephrine action. IV. The influence of epinephrine on lactic acid production and blood sugar utilization. J. Biol. Chem. 84:683. With G. T. Cori. The influence of insulin and epinephrine on glycogen formation in the liver. J. Biol. Chem. 85:275. The rate of absorption of epinephrine from the subcutaneous tissue Science 70:355. 1930 With G. T. Cori and K. W. Buchwald. The mechanism of epinephrine action. VI. Changes in blood sugar, lactic acid, and blood pressure during continuous intravenous injection of epinephrine. Am. J. Physiol. 93:273. With K. W. Buchwald. Effect of continuous intravenous injection of epinephrine on the carbohydrate metabolism, basal metabolism and vascular system of normal men Am. J. Physiol. 95:71. With G. T. Cori and K. W. Buchwald. The mechanism of epinephrine actions. V. Changes in liver glycogen and blood lactic acid after injection of epinephrine and insulin. J. Biol. Chem. 86:375. With E. L. Villaume and G. T. Cori. Studies on intestinal absorption. II. The absorption of ethyl alcohol. J. Biol. Chem. 87:19. With G. T. Cori. Accumulation of a precursor of lactic acid in muscle after epinephrine injections. Proc. Soc. Exp. Biol. Med. 27: 934. 1931 With K. W. Buchwald. The action of epinephrine and insulin in frogs under anaerobic conditions J. Biol. Chem. 92:355. With K. W. Buchwald. The calorigenic action of epinephrine in frogs before and after hepatectomy J. Biol. Chem. 92:367. With G. T. Cori. A method for the determination of hexosemonophosphate in muscle. J. Biol. Chem. 94:561. With G. T. Cori. The influence of epinephrine and insulin injections on hexosemonophosphate content of muscle. J. Biol. Chem. 94: 581. Mammalian carbohydrate metabolism. Physiol. Rev. 11:143.

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Biographical Memoirs: Volume 61 1933 With F. O. Schmitt. Lactic acid formation in medullated nerve. Am. J. Physiol. 106:339. With G. T. Cori. Carbohydrate metabolism. Annu. Rev. Biochem. 2:129. With G. T. Cori. Changes in hexosephosphate, glycogen and lactic acid during contraction and recovery of mammalian muscle. J. Biol. Chem. 99:493. 1934 With G. T. Cori. Carbohydrate metabolism. Annu. Rev. Biochem. 3:151. With G. T. Cori. The disappearance of hexosemonophosphate from muscle under aerobic and anaerobic conditions. J. Biol. Chem. 107:5. 1935 With R. E. Fisher and G. T. Cori. The effect of epinephrine on arterial and venous plasma sugar and blood flow in dogs and cats. Am. J. Physiol. 114:53. With G. T. Cori. Carbohydrate metabolism. Annu. Rev. Biochem. 4:183. With W. M. Shine. The formation of carbohydrate from glycerophosphate in the liver of the rat. Science 82:134. With A. Steiner. The preparation and determination of trehalose in yeast. Science 82:422. 1936 With R. E. Fisher and J. A. Russell. Glycogen disappearance and carbohydrate oxidation in hypophysectomized rats. J. Biol. Chem. 115:627. With G. T. Cori. The formation of hexosephosphate esters in frog muscle. J. Biol. Chem. 116:119. With G. T. Cori. An unusual case of esterification in muscle. J. Biol. Chem. 116:129. With G. T. Cori. Mechanism of formation of hexosemonophosphate in muscle and isolation of a new phosphate ester. Proc. Soc. Exp. Biol. Med. 34:702. 1937 With G. T. Cori and A. H. Hegnauer. Resynthesis of muscle glycogen from hexosemonophosphate. J. Biol. Chem. 120:193. With S. P. Colowick and G. T. Cori. The isolation and synthesis of glucose-1-phosphoric acid. J. Biol. Chem. 121:465.

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Biographical Memoirs: Volume 61 With G. T. Cori. Formation of glucose-1-phosphoric acid in muscle extract. Proc. Soc. Exp. Biol. Med. 36:119. 1938 With G. T. Cori and S. P. Colowick. The formation of glucose-1-phosphoric acid in extracts of mammalian tissues and of yeast. J. Biol. Chem. 123:375. With G. T. Cori and S. P. Colowick. The action of nucleotides in the disruptive phosphorylation of glycogen J. Biol. Chem. 123: 381. With G. T. Cori and S. P. Colowick. The enzymatic conversion of glucose-1-phosphoric ester to 6-ester in tissue extracts. J. Biol. Chem. 124:543. 1939 Enzymatic breakdown and synthesis of carbohydrate. Cold Spring Harbor Symp. Quant. Biol. 7:260. With G. T. Cori and G. Schmidt. The role of glucose-l-phosphate in the formation of blood sugar and synthesis of glycogen in the liver. J Biol. Chem. 129:629. With G. T. Cori. The activating effect of glycogen on the enzymatic synthesis of glycogen from glucose-l-phosphate J. Biol. Chem. 131: 397. With G. Schmidt and G. T. Cori. The synthesis of a polysaccharide from glucose-l-phosphate in muscle extract. Science 89:464. 1940 With S. P. Colowick and M. S. Welch. Glucose oxidation and phosphorylation. J. Biol. Chem. 133:641. With G. T. Cori. The kinetics of the enzymatic synthesis of glycogen from glucose-l-phosphate J. Biol. Chem. 135:733. 1941 With G. T. Cori. Carbohydrate metabolism. Annu. Rev. Biochem. 10:151. With S. P. Colowick and H. M. Kalckar. Glucose phosphorylation and oxidation in cell-free tissue extracts J. Biol. Chem. 137:343. With R. S. Bear. X-ray diffraction studies of synthetic polysaccharides. J. Biol. Chem. 140:111. With E. W. Sutherland and S. P. Colowick. The enzymatic conversion of glucose-6-phosphate to glycogen. J. Biol. Chem. 140:309.

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Biographical Memoirs: Volume 61 1942 With A. A. Green and G. T. Cori. Crystalline muscle phosphorylase. J. Biol. Chem. 142:447. Phosphorylation of carbohydrates. In University of Wisconsin Symposium on Respiratory Enzymes, p. 175. 1943 With G. T. Cori and A. A. Green. Crystalline muscle phosphorylase. III. Kinetics. J. Biol. Chem. 151:39. With G. T. Cori. Crystalline muscle phorphorylase. IV. Formation of glycogen. J. Biol. Chem. 151:57. 1945 With G. T. Cori. The enzymatic conversion of phosphorylase a to b. J. Biol. Chem. 158:321. With G. T. Cori. The activity and crystallization of phosphorylase b. J. Biol. Chem. 158:341. With G. T. Cori and M. W. Slein. Isolation and crystallization of d-glyceraldehyde 3-phosphate dehydrogenase from rabbit muscle. J. Biol. Chem. 159:565. With W. H. Price and S. P. Colowick. The effect of anterior pituitary extract and of insulin on the hexokinase reaction. J. Biol. Chem. 160:633. 1946 With G. T. Cori. Carbohydrate metabolism. Annu. Rev. Biochem. 15:193. Enzymatic reactions in carbohydrate metabolism. In Harvey Lect. Series no. 41, 253. With L. Berger, M. W. Slein, and S. P. Colowick. Isolation of pure hexokinase from yeast. J. Genet. Physiol. 29:141. 1947 With M. E. Krahl. The uptake of glucose by the isolated diaphragm of normal, diabetic, and adrenalectomized rats. J. Biol. Chem. 170:607. 1948 With W. E. Sutherland. Influence of insulin preparations on glycogenolysis in liver slices J. Biol. Chem. 172:737. With M. A. Swanson. Studies on the structure of polysaccharides. III. Relation of structure to activation of phosphorylase. J. Biol. Chem. 172:815.

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Biographical Memoirs: Volume 61 With G. T. Cori and M. W. Slein. Crystalline d-Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. J. Biol. Chem. 173:605. With J. F. Taylor, S. F. Velick, G. T. Cori, and M. W. Slein. The prosthetic group of crystalline d-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 173:619. 1949 With G. T. Cori. Polysaccharide phosphorylase. In Les Prix Nobel en 1947, p. 216. Stockholm: Imprimerie Royal. With E. W. Sutherland and T. Z. Posternak. The mechanism of action of phosphoglucomutase. J. Biol. Chem. 179:501. With E. W. Sutherland, R. Haynes, and N. S. Olsen. Purification of the hyperglycemic-glycogenolytic factor from insulin and from gastric mucosa. J. Biol. Chem. 180:825. With E. W. Sutherland, M. Cohn, and T. Posternak. The mechanism of the phosphoglucomutase reaction. J. Biol. Chem. 180:1285. With E. W. Sutherland and T. Posternak. Mechanism of the phosphoglyceric mutase reaction. Biol. Chem. 181:153. 1950 With S. F. Velick and G. T. Cori. The combination of diphosphopyridine nucleotide with glyceraldehyde phosphate dehydrogenase. Biochim. Biophys. Acta 4:160. 1951 With G. T. Cori, S. Ochoa, and M. W. Slein. The metabolism of fructose in liver. Isolation of fructose-1-phosphate and inorganic pyrophosphate. Biochim. Biophys. Acta 7:304. With E. W. Sutherland. Effect of hyperglycemic-glycogenolytic factor and epinephrine on liver phosphorylase. J. Biol. Chem. 188:531. 1952 With J. Larner, B. Illingworth, and G. T. Cori. Structure of glycogens and amylopectins. II. Analysis by stepwise enzymatic degradation. J. Biol. Chem. 199:641. With G. T. Cori. Glucose-6 phosphatase of liver in glycogen storage disease. J. Biol. Chem. 199:661. 1956 With E. Helmreich. Some problems of permeability of tissue cells to sugar. Ciba Found. Colloq. Endocrinol. 9:227.

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Biographical Memoirs: Volume 61 With B. Illingworth and G. T. Cori. Amylo-1, 6-glucosidase in muscle tissue in generalized glycogen storage disease. J. Biol. Chem. 218: 123. With N. B. Madsen. The interaction of muscle phosphorylase with p-chloromercuribenzoate. I. Inhibition of activity and effect on the molecular weight. J. Biol. Chem. 223:1055. 1957 With N. B. Madsen. The binding of adenylic acid by muscle phosphorylase. J. Biol. Chem. 224:899. 1958 With B. Illingworth, H. S. Jansz, and D. H. Brown. Observations on the function of pyridoxal-5-phosphate in phosphorylase Proc. Natl. Acad. Sci. USA 44:1180. 1959 With R. Hauk, B. Illingworth, and D. H. Brown. Enzymes of glycogen synthesis in glycogen-deposition disease. Biochim. Biophys. Acta 33:554. With D. M. Kipnis and E. Helmreich. Studies of tissue permeability. IV. The distribution of glucose between plasma and muscle. J. Biol. Chem. 234:165. 1960 With D. M. Kipnis. Studies of tissue permeability. VI. The penetration and phosphorylation of 2-deoxyglucose in the diaphragm of diabetic rats. J. Biol. Chem. 235:3070. 1961 With D. H. Brown and B. Illingworth. The mechanism of the de novo synthesis of polysaccharide by phosphorylase. Proc. Natl. Acad. Sci. USA 47:479. Control mechanisms in the utilization of glucose. Proc. Robert A. Welch Found. Conf. Chem. Res. 5:247. 1962 With W. H. Danforth and E. Helmreich. The effect of contraction and of epinephrine on the phosphorylase activity of frog sartorius muscle. Proc. Natl. Acad. Sci. USA 48:1191.

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Biographical Memoirs: Volume 61 1963 With D. H. Brown and B. Illingworth. Enzymatic debranching of glycogen: A new pathway in rabbit muscle for the enzymatic debranching of glycogen. Nature 197:979. With R. A. Field. The relationship between glucose load and utilization in normal and diabetic rats. In Perspectives in Biology, ed. V. G. Foglia, L. F. Leloir, and S. Ochoa, p. 162. Amsterdam: Elsevier. 1964 With S. Karpatkin and E. Helmreich. Regulation of glycolysis in muscle. II Effect of stimulation and epinephrine in isolated frog sartorius muscle. J. Biol. Chem. 239:3139. With E. Helmreich. The role of adenylic acid in the activation of phosphorylase. Proc. Natl. Acad. Sci. USA 51:131. 1965 With B. Illingworth. Glucose-6-phosphate and pyrophosphatase activities of homogenates of livers from patients with glycogen storage disease. Biochem. Biophys. Res. Commun. 19:10. With E. Helmreich. Regulation of glycolysis in muscle. Adv. Enzyme Regul. 3:91. 1966 With D. H. Brown and B. Illingworth Brown. Effect of changes in the outer structure of glycogen on the debranching activity of the transferase-glucosidase system. Arch. Biochem. Biophys. 116:479. With S. Karpatkin and E. Helmreich. Regulation of glycolysis in muscle. IV. Effects of anaerobiosis, insulin, and electrical stimulation on the penetration and phosphorylation of 2-deoxyglucose in isolated frog sartorius muscle. In Current Aspects of Biochemical Energetics, ed. N. O. Kaplan and E. P. Kennedy, p. 127. New York: Academic Press. With E. Helmreich. The activation of glycolysis in frog sartorius muscle by epinephrine Pharmacol. Rev. 18:189. 1968 With H. T. Narahara. Hormonal control of carbohydrate metabolism in muscle. In Carbohydrate Metabolism and Its Disorders, ed. E. Dickens, P. J. Randle, and W. J. Whelan, p. 375. New York: Academic Press.

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Biographical Memoirs: Volume 61 With R. P. Erickson and S. Glüecksohn-Waelsch. Glucose-6-phosphatase deficiency caused by radiation-induced alleles at the albino locus in the mouse. Proc. Natl. Acad. Sci. USA 59:437. 1969 The call of science. Annu. Rev. Biochem. 38:1. With J. D. Russell and S. Glüecksohn-Waelsch. Further studies on the x-ray-induced genetic loss of glucose-6-phosphatase in liver and kidney of mice. FEBS Symp. 19:315. 1970 With S. Glüeckson-Waelsch. Glucose-6-phosphatase deficiency: Mechanisms of genetic control and biochemistry. Biochem. Genet. 4:194. The molecular properties of phosphorylase. In Perspectives in Biological Chemistry, ed. R. E. Olsen, p. 181. New York: Marcel Dekker. 1971 Some thoughts on the relation between science and the humanities. In Proceedings of the First International Humanistic Symposium, Delphi , p. 304. Athens: Hellenic Society for Humanistic Studies. 1972 With R. C. Garland. Separation of phospholipids from glucose-6-phosphatase by gel chromatography Specificity of phospholipid reactivation. Biochemistry 11:4712. Some salient features of the enzymatic synthesis of the glycosidic bond. In Biochemistry of the Glycosidic Linkage, p. 765. Proceedings of the Pan-American Association of Biochemical Societies Symposium, vol. 2. New York: Academic Press. 1973 With J. Thorndike, M. J. Trigg, R. Stockert, and S. Glüecksohn-Waelsch. Multiple biochemical effects of a series of x-ray-induced mutations at the albino locus in the mouse. Biochem. Genet. 9:25. With R. C. Garland and H. W. Chang. Purification of particulate glucose-6-phosphatase. Biochemistry 12:3126. 1974 With S. Glüecksohn-Waelsch, M. B. Schiffman, and J. Thorndike. Complementation studies of lethal alleles in the mouse causing deficiencies of glucose-6-phosphatase, tyrosine aminotransferase, and serine dehydratase Proc. Natl. Acad. Sci. USA 71:825.

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Biographical Memoirs: Volume 61 With R. C. Garland and H. W. Chang. Relipidation of phospholipid-depleted microsomal particles with high glucose 6-phosphatase activity. Proc. Natl. Acad. Sci. USA 71:3805. 1976 With E. Helmreich, H. P. Zenner, and T. Pfeuffer. Signal transfer from hormone receptor to adenylate cyclase. In Current Topics in Cellular Regulation, vol. 10, ed. B. L. Horecker and E. R. Stadtman, p. 41. New York: Academic Press. With R. C. Garland and H. W. Chang. The effect of p-hydroxy-mercuribenzoate and congeners on microsomal glucose-6-phosphatase. Mol. Cell. Biochem. 12:23. Gerty Theresa Cori, 1896-1957. In American Chemists and Chemical Engineers, ed. W. D. Miles, p. 94. Washington, D.C.: American Chemical Society Press. There can be no moratorium on science. In International Conference on the Responsibility of Science in Modern Society, p. 11. Florence, Italy. With R. C. Garland, J. Satrustegui, and S. Glüecksohn-Waelsch. Deficiency in plasma protein synthesis caused by x-ray-induced lethal albino alleles in mouse. Proc. Natl. Acad. Sci. USA 73:3376. The role of lactic acid in the development of biochemistry. In Reflections on Biochemistry, ed. A. Kornberg et al., p. 17. Oxford: Pergamon Press. 1980 With S. Glüecksohn-Waelsch, L. S. Teicher, and L. Pick. Genetic rescue of lethal genotypes in the mouse. Dev. Genet. 1:219. 1981 With S. Glüecksohn-Waelsch, H. P. Klinger, L. Pick, S. L. Schlagman, L. S. Teicher, and H.-F. Wang Chang. Complementation of gene deletions by cell hybridization. Proc. Natl. Acad. Sci. USA 78:479. The glucose-lactic acid cycle and gluconeogenesis. In Current Topics in Cellular Regulation, vol. 18, ed. R. W. Estabrook and P. A. Srere, p. 377. New York: Academic Press. With R. C. Garland. Protein synthesis with membrane-bound polysomes and albumin messenger RNA from livers of mutant mice. Mol. Cell. Biochem. 36:29. 1983 With S. Glüecksohn-Waelsch, P. A. Shaw, and C. Robinson. Correction of a genetically caused enzyme defect by somatic cell hybridization. Proc. Natl. Acad. Sci. USA 80:6611.