Zusammenfassung
Für den Biochemiker hat die lebendige Zelle drei einzigartige Eigenschaften, die als ein Hauptcharakteristikum des Lebens angesehen werden müssen1:
-
1.
Eine Vielfalt von makro- und mikromolekularen chemischen Verbindungen hat sich in der Zelle zu einer zusammenwirkenden Einheit verbunden.
-
2.
Das Leben in der Zelle wird nur aufrechterhalten durch das stetige Reagieren dieser Stoffe miteinander, durch Auf- und Abbau und durch Beziehungen dieses Stoffwechsels mit der Außenwelt. Der Aufbau, der den Abbau oft überwiegt, kann sich nur durch ständige Stoffzufuhr von außen vollziehen.
-
3.
Dieses dynamische Stoffwechselgeschehen der Zelle, bei dem sich die einzelnen Stoffgruppen immer wieder gegenseitig ergänzen, hat eine große Möglichkeit der Variabilität. Diese wird regiert durch einen wunderbaren, sinnvollen, aber komplizierten Regulations-Mechanismus, auf dessen Wirksamkeit das Leben wesentlich beruht.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Literatur
Albert, A., C. W. Rees and A. J. H. Tomllxsox: The influence of chemical constitution on antibacterial activity. Part Viii. 2-mercaptopyridine-N-oxide and some general observations on metal binding agents. Brit. J. exp. Path. 37, 500 (1956).
Allfrey, V. G.: Observations on the mechanism and control of protein synthesis in the cell nucleus. 5. Internat. Kongr. für Biochemie, Moskau 1961. Symposium II, Preprint 140, 1 (1961).
Amarasingham, C., and H. E. Umbarger: The effect of glucose on oxalacetic carboxylase in two strains of Escherichia coli. Bact. Proc. 55, 115 (1955).
Amoore, J. E.: The permeability of isolated rat-liver mitochondria at 0° to the metabolites pyruvate, succinate, citrate, phosphate, adenosine-5-phosphate and adenosine triphosphate. Biochem. J. 70, 718 (1958).
Ashida, J., and M. Imai: Origin of copper resistant cells. Studies on the adaptation of yeast to copper. XV. Bot. Mag. (Tokyo) 69, 560 (1956).
Astrachan, L., and E. Volkin: Effects of chloramphenicol on ribonucleic acid metabolism in T2-infected Escherichia coli. Biochim. biophys. Acta 32, 449 (1959).
Bagdasarian, G.: L’influence de la streptomycine sur la production de la penicillinase induite chez B. cereus. Ann. Inst. Pasteur 99, 150 (1960).
Baker, R. S., J. E. Johnson and S. W. Fox: Incorporation of p-fluorophenylalanine into proteins of Lactobacillus arabinosus. Biochim. biophys. Acta 28, 318 (1958).
Balassa, R.: Einige Bedingungen der Ausbildung einer durch Desoxyribonukleinsäuren induzierten niedrigen Streptomycinresistenz bei Rhizobien. Acta microbiol. Acad. Sci. hung. 4, 85 (1957).
Bardarov, S.: Untersuchungen über die Biosynthese der Penicillinase. Arch. Mikrobiol. 29, 143 (1958).
Barker, S. A., E. J. Bourne and O. Theander: Studies of Aspergillus piger. Part V. The enzymic synthesis of a new trisaccharide. J. them. Soc. 1957, P. I I, 2064 (1957).
Barnard, E. A., and W. D. Stein: Some relations between enzyme activity, chemical reactivity and urea-induced disorientations in ribonuclease. Biochim. biophys. Acta 37, 371 (1960).
Barner, H. D., and S. S. Cohen: The relation of growth to the lethal damage induced by ultraviolet irradiation in Escherichia coli. J. Bact. 71, 149 (1956).
Barner, H. D., and S. S. Cohen: Protein synthesis and Rna turnover in a pyrimidine deficient bacterium. Mit Addendum von D. Kanazir: Addendum: The apparent mutagenicity of thymine deficiency. Biochim. biophys. Acta 30, 12 (1958).
Barnum, C. P., and R. A. Huseby: The intracellular heterogeneity of pentose nucleic acid as evidenced by the incorporation of radiophosphorus. Arch. Biochem. 29, 7 (1950).
Barret, J. T., A. D. Larson and R. E. Kallio: The nature of the adaptive lag of Pseudolamas fluorescens toward citrate. J. Bact. 65, 187 (1953).
Benzer, S.: Induced synthesis of enzymes in bacteria analysed at the cellular level. Biochim. biophys. Acta 11, 383 (1953).
Bergmann, E. D., and S. Sicher: Mode of action of chloramphenicol. Nature (Lond.) 170, 931 (1952).
Bernheim, F.: Rapid reversal of ethionine inhibition of enzyme induction in Pseudomonas aeruginosa by L- and n-methionine. Proc. Soc. exp. Biol. (N.Y.) 101, 346 (1959).
Bertrand, D., et A. DE Wolf: Le zinc, oligo élément dynamique indispensable à la synthèse de la phosphofructokinase et de la glycéraldéhyde-phosphate déhydrogénase de l’Aspergillus niger. C. R. Acad. Sci. (Paris) 246, 2537 (1958).
Beyer, R. E.: Evidence in support of two adenosin triphosphatase pathways in rat-liver mitochondria. Biochim. biophys. Acta 32, 588 (1959).
Black, A. L., and M. Kleiber: The recovery of norleucine from casein after administering norleucine-3-C14 to intact cows. J. Amer. chem. Soc. 77, 6082 (1955).
Black, S., and N. G. Wright: ß-aspartokinase and ß-aspartiphosphate. J. biol. Chem. 213, 27 (1955).
Black, S., and N. G. Wright: Aspartic ß-semialdehyde dehydrogenase and aspartic ß-semialdehyde. J. biol. Chem. 213, 39 (1955).
Black, S., and N. G. Wright: Homoserine dehydrogenase. J. biol. Chem. 213, 51 (1955).
Bolton, E. T., and H. G. Mandel: The effects of 6-mercaptopurine on biosynthesis in Escherichia coli. J. biol. Chem. 227, 833 (1957).
Bonner, D. M., Y. Suyama and J. A. DE Moss: Genetic fine stucture and enzyme formation (Symposium). Fed. Proc. 19, 926 (1960).
Boyer, P. D., H. Lardy and K. MyrbÄCK: The enzymes. 2nd edit.: 4 volumes, vol. I. New York: Academic Press 1959.
Boyer, P. D., and M. P. Stulberg: Tracing of the in vivo path from amino acid to protein. Proc. nat. Acad. Sci. (Wash.) 44, 92 (1958).
Bradfield, J. R. G.: Organization of bacterial cytoplasms. In: Bacterial Anatomy. Symp. Soc. gen. Microbiol. 6, 296 (1956).
Brawerman, G., and M. YèAs: Incorporation of the amino acid analog tryptazan into the protein of Escherichia coli. Arch. Biochem. 68, 112 (1957).
Bresnick, E., S. Singer and G. H. Hitchings: Mechanism of action of 6-azacytosine in bacteria. Biochim. biophys. Acta 37, 251 (1960).
Britten, R. J., R. B. Roberts and E. F. French: Amino acid adsorption and protein synthesis in Escherichia coli. Proc. nat. Acad. Sci. (Wash.) 41, 863 (1955).
Brookes, P., A. R. Crathorn and G. D. Hunter: The incorporation of labelled amino acids into protein by isolated cytoplasmic membrans of Bacillus megaterium. Intermediate reactions. Biochem. J. 71, 31 (1959).
BuChner, P.: Praktikum der Zellenlehre. Teil 1: Allgemeine Zellen-und Befruchtungslehre (Sammlung naturw. Praktika, Bd. 5 ). Berlin: Gebrüder Borntraeger 1915.
Bussard, A., S. Naono, F. Gros et J. Monod: Effets d’un analogue de l’uracile sur les propriétés d’une protéine enzymatique synthétisée en sa présence. C. R. Acad. Sci. (Paris) 250, 4049 (1960).
Campbell, A.: Effect of starvation for glucose during reversion of a long term adapting yeast. J. Bact. 74, 553 (1957).
Campbell, A. M., and S. Spiegelman: The growth kinetics of elements necessary for galactozymase formation in “long term adapting” yeasts.C. R.Lab.Carlsberg, Sér. physiol. 26, 13 (1956).
Canellakis, E. S.: Some aspects of the metabolism in vitro of 2-C14-labelled orotic acid, uracil, uridine and uridylic acid. Fed. Proc. 14, 324 (1955).
Canellakis, E. S.: Biosynthesis of uracil nucleotides. Fed. Proc. 15, 229 (1956).
Canellakis, E. S.: Pyrimidine metabolism. I. Enzymatic pathways of uracil and thymine degradation. J. biol. Chem. 221, 315 (1956).
Canellakis, E. S.: Incorporation of radioactive uridine-5’-monophosphate into ribonucleic acid by soluble mammalian enzymes. Biochim. biophys. Acta 23, 217 (1957).
Chambers, C. W., H. H. Tabak and P. W. Kabler: Effect of Krebs cycle metabolites on the viability of Escherichia coli treated with heat and chlorine. J. Bact. 73, 77 (1957).
Chance, B.: Enzyme mechanisms in living cells. In: The mechanism of enzyme action (W. D. Mcelroy and B. Glass, eds.), p. 399. Baltimore: Johns Hopkins Press 1954.
Chance, B.: Enzymes in action in living cells: the steady state of reduced pyridine nucleotides. Harvey Lect. 49, 145 (1955).
Chance, B., and G. R. Williams: The respiratory chain and oxidative phosphorylation. Advanc. Enzymol. 17, 65 (1956).
Ceantrenne, H.: Nucleic acid metabolism and induced enzyme formation. Rec. Tray. chim. Pays-Bas 77, 586 (1958).
Ceantrenne, H.: Newer developments in relation to protein biosynthesis. Ann. Rev. Biochem. 27, 35 (1958).
Ceantrenne, H.: Remarques sur l’inhibition de la synthèse des protéines par l’azaguanine. 4th Internat. Congr. Biochem., Vienna 1958, Sympos. 8, 197 (1960).
Ceantrenne, H., and S. Devreux: Dissociation of the synthesis of nucleic acids from the synthesis of protein by a purine analogue. Exp. Cell Res., Suppl. 6, 152 (1958).
Ceantrenne, H., and S. Devreux: Action de la 8-azaguanine sur Bacillus cereus. Arch. int. Physiol. 66, 114 (1958).
Ceantrenne, H., and S. Devreux: Formation induite de catalase et métabolisme des acides nucléiques chez la levure. Effet des rayons X. Biochim. biophys. Acta 31, 134 (1959).
Ceantrenne, H., and S. Devreux: Action de la 8-azaguanine sur la synthèse des protéines et des acides nucléiques chez Bacillus cereus. Biochim. biophys. Acta 39 486 (1960 a).
Ceantrenne, H., and S. Devreux: Restauration de la synthèse d’enzymes après inhibition par l’azaguanine. Biochim. biophys. Acta 41 239 (1960 b).
Clarke, J. S., and C. A. Pasternak: The regulation of amino sugar metabolism in Bacillus subtilis. Biochem. J. 81, 1 P (1961).
Clayton, R. K.: Protein synthesis in the induced formation of catalase in Rhodopseudomonas spheroides. J. biol. Chem. 235, 405 (1960).
Clayton, R. K.: The induced synthesis of catalase in Rhodopseudomonas spheroides. Biochim. biophys. Acta 37, 503 (1960).
Cohen, G. N., et D. B. Cowie: Remplacement total de la méthionine par la sélénométhionine dans les protéines d’Escherichia coli. C. R. Acad. Sci. (Paris) 244, 680 (1957).
Cohen, G. N., and J. Monod: Bacterial permeases. Bact. Rev. 21, 169 (1957).
Cohen, G. N., et H. V. Rickenbero: Existence d’accepteurs spécifiques pour les amino-acides chez Escherichia coli. C.R. Acad. Sci. (Paris) 240, 2086 (1955).
Cohen, G. N., et H. V. Rickenbero: Concentration spécifique réversible des amino acids chez Escherichia coli. Ann. Inst. Pasteur 91, 693 (1956).
Cohen, S. S.: Streptomycin and desoxyribonuclease in the study of variations in the properties of a bacterial virus. J. biol. Chem. 166, 393 (1946).
Coln, M.: On the inhibition by glucose of the induced synthesis of ß-galactosidase in Escherichia coli. Henry Ford Hospital Intern. Sympos: Enzymes. Units of biological structure and function (edit. Garbler), p. 41. New York: Acad. Press 1956.
Coln, M.: Contributions of studies on the ß-galactosidase of Escherichia coli to our understanding of enzyme synthesis. Bact. Rev. 21, 140 (1957).
Coln, M., G. N. Cohen et J. Monod: L’effet inhibiteur spécifique de la méthionine dans la formation de la méthionine-synthétase chez E. coli. C.R. Acad. Sci. (Paris) 236, 746 (1953).
Coln, M., and K. Horibata: Inhibition by glucose of the induced synthesis of the ß-galactosidaseenzyme system of E. coli. Analysis of maintenance. J. Bact. 78, 601 (1959).
Coln, M.: Analysis of the differentiation and of the heterogeneity within a population of E. coli untergoing induced ß-galactosidase synthesis. J. Bact. 78, 613 (1959).
Coln, M.: Physiology of the inhibition by glucose of the induced synthesis of the ß-galactosideenzyme system of Escherichia. J. Bact. 78, 624 (1959).
Coln, M., E. Lennox and S. Spiegelman: On the behaviour of the E. coli Pz-“ß-galactosidesystem” introduced into Shigella dysenteriae. Biochim. biophys. Acta 39, 255 (1960).
Coln, M., E. Lennox, and J. Moxod: Specific inhibition and induction of enzyme biosynthesis. In: Adaptation in microorganisms. 3rd Sympos. Soc. for gen. Microbiol., p. 138. Cambridge: Cambridge Univ. Press. 1953.
Cowie, D. B., and G. N. Cohen: Biosynthesis by E. coli of active altered proteins containing selenium instead of sulfur. Biochim. biophys. Acta 26, 252 (1957).
Cowie, D. B., and G. N. Cohen, E. T. Bolton and H. DE Robichon-SzUlmajster: Amino acid analog incorporation into bacterial proteins. Biochim. biophys. Acta 34, 39 (1959).
Crane, R. K., and A. Sors: The non-competitive inhibition of brain hexokinase by glucose6-phosphate and related compounds. J. biol. Chem. 210, 597 (1954).
Crathorn, A. R., and G. D. Hunter: Amino acid “exchange” and protein synthesis in cell walls of Bacillus megaterium. Biochem. J. 69, 47 (1958).
Crawford, I., A. Kornberg and E. S. Simms: Conversion of uracil and orotate to uridine 5-phosphate by enzymes in Lactobacilli. J. biol. Chem. 226, 1093 (1957).
Crawford, I. P.: Identification of the triose phosphate formed in the tryptophan synthetase reaction. Biochim. biophys. Acta 45, 405 (1960).
Creaser, E. H.: The assimilation of amino acids by bacteria. 22. The effect of 8-azaguanine upon enzyme formation in Staphylococcus aureus. Biochem. J. 64, 539 (1956).
Danielli, J. F.: Structural factors in cell permeability and secretion. VI. Structural aspects of cell physiology. Symp. Soc. exp. Biol. 6, 1 (1952).
Datta, S. P., and B. R. Rabin: The chelation of metal ions by dipetides and related compounds. Biochim. biophys. Acta 19, 572 (1956).
Davie, E. W., V. V. Koningsberger and F. Lipmann: The isolation of a tryptophan-activating enzyme from pancreas. Arch. Biochem. 65, 21 (1956).
Davis, B. D.: Relations between enzymes and permeability (membrane transport) in bacteria. Henry Ford Hospital Intern. Sympos.: Enzymes. Units of biological structure and function (edit. Gaebler), p. 509. New York: Acad. Press 1956.
de Ley, J., and J. Schel: Studies on the metabolism of Acetobacter peroxydans. II. The enzymic mechanism of lactate metabolism. Biochim. biophys. Acta 35, 154 (1959).
de Moss, J. A., and G. D. Novelli: An amino acid dependent exchange between inorganic pyrophosphate and ATP in microbial extracts. Biochim. biophys. Acta 18, 592 (1955).
DE Moss, J. A., and G. D. Novelli: An amino acid dependent exchange between P32-labelled inorganic pyrophosphates and ATP in microbial extracts. Biochim. biophys. Acta 22, 49 (1956).
Dénes, G.: Glucose repression and induction of ß-galactosidase synthesis in Escherichia coli. Biochim. biophys. Acta 50, 408 (1961).
Dixon, M.: Multi-enzyme systems. 4 Lectures, London 1948. Cambridge: Cambridge Univ. Press, 2nd Print 1951.
Doudney, C. O., and F. L. Haas: Chloramphenicol, nucleic acid synthesis and mutation induced by ultraviolet light. Biochim. biophys. Acta 40, 375 (1960).
Dressler, H., and C. R. Dawson: On the nature and mode of action of the copper-protein, tyrosinase. I. Exchange experiments with radioactive copper and the resting enzyme. Biochim. biophys. Acta 45, 508 (1960a).
Dressler, H., and C. R. Dawson: On the nature and mode of action of the copperprotein, tyrosinase. II. Exchange experiments with radioactive copper and the functioning enzyme. Biochim. biophys. Acta 45, 515 (1960b).
Duerrsen, J. D., and H. Halvorson: Purification and properties of an inducible ß-glucosidase of yeast. J. biol. Chem. 233, 1113 (1958).
Durham, N. N., and D. L. Mcpherson: Influence of extraneous carbon sources on biosynthesis de novo of bacterial enzymes. J. Bact. 80, 7 (1960).
Dutton, G. J.: The mechanism of glucuronide formation: a review. Biochem. J. 73, 29 (1959).
Elson, D.: Latent ribonuclease in a ribonucleoprotein. Biochim. biophys. Acta 27, 216 (1958).
Elson, D.: Preparation and properties of a ribonucleoprotein isolated from Escherichia coli. Biochim. biophys. Acta 36, 362 (1959).
Elson, D.: Latent enzymic activity of a ribonucleoprotein isolated from Escherichia coli. Biochim. biophys. Acta 36, 372 (1959).
Engelsberg, E.: Glucose inhibition and the diauxie phenomenon. Proc. nat. Acad. Sci. (Wash.) 45, 1494 (1959).
Flavin, M., and T. Koxo: Threonine synthetase mechanism: studies with isotopic oxygen. J. biol. Chem. 235, 1109 (1960).
Fukumoto, J., T. Yamamoto and D. Tsuru: Effects of carbon sources and base analogues of nucleic acid on the formation of bacterial amylase. Nature (Lond.) 180, 438 (1957).
Gale, E. F.: Points of interference by antibiotics in the assimilation of amino acids by bacteria. 2e Congr. Internat. de Biochimie, Paris 1952. Sympos. sur le mode d’action des antibiotiques, Paris, p. 1, 1952.
Gale, E. F.: Assimilation of amino acids by gram-positive bacteria and some actions of antibiotics thereon. Advanc. Protein Chem. 8, 285 (1953).
Gale, E. F.: Incorporation of amino acids by disrupted staphylococci: replacement of ribonucleic acid by its digestion products. Proc. 3rd Internat. Congr. Biochem., Brussells 1955, p. 345. New York: Academic Press 1956.
Gale, E. F.: The biochemical organization of the bacterial cell. Proc. roy. Soc. B 146, 166 (1957).
Gale, E. F.: Specific inhibitors of protein synthesis. 8th Sympos. Soc. Gen. Microbiol., London 1958: The strategy of chemotherapy, p. 212. Cambridge: Cambridge Univ. Press 1958.
Gale, E. F., and J. P. Folkes: The assimilation of amino acids by bacteria. 15. Actions of antibiotics on nucleic acid and protein synthesis in Staphylococcus aureus. Biochem. J. 53, 493 (1953).
Gale, E. F., and J. P. Folkes: The assimilation of amino acids by bacteria. 19. The inhibition of phenylalanine incorporation in Staphylococcus aureus by chloramphenicol and p-chlorphenylalanine. Biochem. J. 55, 730 (1953).
Gale, E. F., and J. P. Folkes: The assimilation of amino acids by bacteria. 20. The incorporation of labelled amino acids by disrupted staphylococcal cells. Biochem. J. 59, 661 (1955).
Gale, E. F., and J. P. Folkes: The assimilation of amino acids by bacteria. 21. The effect of nucleic acids on the development of certain enzymic activities in disrupted staphylococcal cells. Biochem. J. 59, 675 (1955).
Gale, E. F., and E. S. Taylor: The assimilation of amino acids by bacteria. 5. The action of penicillin in preventing the assimilation of glutamic acid by Staphylococcus aureus. J. gen. Microbiol. 1, 314 (1947).
Gorini, L.: Regulation en retour (feedback control) de la synthèse de l’arginine chez Escherichia coli. Bull. Soc. Chim. biol. (Paris) 40, 1939 (1958).
Gorini, L.: Antagonism between substrate and repressor in controlling the formation of a biosynthetic enzyme. Proc. nat. Acad. Sci. (Wash.) 46, 682 (1960).
Gorini, L., and W. Gundersen: Induction by arginine of enzymes of arginine biosynthesis in Escherichia coli B. Proc. nat. Acad. Sci. (Wash.) 47, 961 (1961).
Gorini, L., and W. K. Maas: The potential for the formation of a biosynthetic enzyme in Escherichia coli. Biochim. biophys. Acta 25. 208 (1957).
Gorini, L., and W. K. Maas: Feedback control of the formation of biosynthetic enzymes. Symposium on the chemical basis of development (McElroy and Glass, eds.), p. 469. Baltimore: Johns Hopkins Press 1958.
Gros, FR., et F. Gros: Rôle des aminoacides dans la synthèse des acides nucléiques chez Escherichia coli. Biochim. biophys. Acta 22, 200 (1956).
Gros, FR., et F. Gros: Rôle des acides aminés dans la synthèse des acides nucléiques chez Escherichia coli. Exp. Cell Res. 14, 104 (1958).
Gross, D., and H. Tarver: Studies on ethionine. IV. The incorporation of ethionine into the proteins of tetrahymena. J. biol. Chem. 217, 169 (1955).
Gross, S. R.: Enzymatic autoinduction and the hypothesis of intracellular permeability barriers in Neurospora. Trans. N.Y. Acad. Sci., Ser. I I, 22, 44 (1959).
Gross, S. R., and A. Fein: Linkage and function in Neurospora. Genetics 45, 885 (1960).
GRÜNberg-Manago, M., and S. Ochoa: Enzymatic synthesis and breakdown of polynucleotides; polynucleotide phosphorylase. J. Amer. them. Soc. 77, 3165 (1955).
Gross, S. R., P. J. Ortiz and S. Ochoa: Enzymatic synthesis of nucleic acidlike polynucleotides. Science 122, 907 (1955).
Gross, S. R., P. J. Ortiz and S. Ochoa: Enzymatic synthesis of polynucleotides. I. Polynucleotide phosphorylase of Azotobacter vinelandii. Biochim. biophys. Acta 20, 269 (1956).
Grylls, F. S. M., and J. S. Harrison: Adaptation of yeast to maltose fermentation. Nature (Lond.) 178, 1471 (1956).
Hahn, F E., and C. L. Wisseman: Inhibition of adaptive enzyme formation by antimicrobial agents. Proc. Soc. exp. Biol. (N.Y.) 76, 533 (1951).
Hahn, F E., C. L. Wisseman, and H. E. Hours: Mode of action of chloramphenicol. II. Inhibition of bacterialD-polypeptide formation of an L-stereoisomer of chloramphenicol. J. Bact. 67, 674 (1954).
Hahn, F E., C. L. Wisseman, and H. E. Hours: Mode of action of chloramphenicol. Iii. Action of chloramphenicol on bacterial energy metabolism. J. Bact. 69, 215 (1955).
Hakim, A. A.: Tryptophan-tryptophanase adaptation. II. Action of penicillin, streptomycin, tetracyn and chloramphenicol on certain enzyme systems influencing enzyme adaptation. Enzymologia 19, 130 (1958).
Hall, J. B., and F. W. Allen: Studies on the incorporation of orotic acid into the 5-ribosyluracil phosphate of the ribonucleic acids of yeast. Biochim biophys. Acta 39, 557 (1960).
Hall, J. B., and F. W. Allen: Studies on the biosynthesis of 5-ribosyluracil phosphate in Neurospora crassa 36601. Biochim. biophys. Acta 45, 163–171 (1960).
Halvorson, H., S. Spiegelman and R. L. Hinman: The effect of tryptophan analogs on the induced synthesis of maltase and protein synthesis in yeast. Arch. Biochem. 55, 512 (1955).
Hamers, R., and C. Hamers-Casterman: Synthesis by Escherichia coli of a ß-galactosidaselike protein under the influence of thiouracil. Biochim. biophys. Acta 33, 269 (1959).
Hamilton, W. A., and E. A. Dawes: A diauxic effect with Pseudomonas aeruginosa. Biochem. J. 71, 25 (1959).
Harrington, M.: The action of antibiotics on Bacterium coli. Thesis, Nation. Univ. of Ireland, Univ. College, Cork 1955.
Heinz, E.: Aktiver Transport von Aminosäuren. 12. Colloquium der Ges. für Physiol. Chemie, Mosbach/Baden, 1961, S. 167. Berlin- Göttingen-Heidelberg: Springer 1961.
Herbert, E., and E. S. Canellakis: Studies on synthesis of soluble ribonucleic acid. Iii. Analytic studies on soluble ribonucleic acid of rat. Biochim. biophys. Acta 42, 363 (1960).
Herzenberg, L. A.: Studies on the induction of ß-galactosidase in a cryptic strain of Escherichia coli. Biochim. biophys. Acta 31, 525 (1959).
Hoch, F. L., R. J. P. Williams and B. L. Vallee: The role of zinc in alcohol dehydrogenase. II. The kinetics of the instantaneous reversible inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline. J. biol. Chem. 232, 453 (1958).
Holmes, R., R. Sheinin and B. F. Crocker: A study of the permeability barrier to ß-galactosides in Escherichia coli B. Canad. J. Biochem. 39, 45 (1961).
Holzer, H.: Über Fermentketten und ihre Bedeutung für die Regulation des Kohlenhydratstoffwechsels in lebenden Zellen. In: Biologie und Wirkung der Fermente. 4. Colloquium der Ges. für Physiol. Chemie, S. 89. Berlin-Göttingen-Heidelberg: Springer 1953.
Holzer, H.: Kinetik und Thermodynamik enzymatischer Reaktionen in lebenden Zellen und Geweben. In: Ergebnisse der Medizinischen Grundlagenforschung (Hrsg. Bauer), Bd. I, S. 189. Stuttgart: Georg Thieme 1956.
Holzer, H.: Enzymic regulation of fermentation in yeast cells. Ciba Foundation Symposium on the regulation of cell metabolism, p. 277. London: J. &. A. Churchill Ltd. 1959.
Holzer, H.: Carbohydrate metabolism. Ann. Rev. Biochem. 28, 171 (1959).
Holzer, H., u. R. Freytag-Hilf: Zusammenwirken der Gärungsenzyme beim anaeroben und aeroben Glucoseumsatz in Hefezellen. Hoppe-Seylers Z. physiol. Chem. 316, 7 (1959).
Holzer, H., u. A. Holldorf: Enzymatische Regulation von Atmung und Gärung. In Handbuch der
Pflanzenphysiologie, Bd. Xii /1, S. 1092. Berlin-Göttingen-Heidelberg: Springer 1959.
Holzer, H., u. I. Witt: Regulation des Pentosephosphat-Cyklus durch Tpnh-Oxydation. Angew. Chem. 70, 439 (1958).
Holzer, H., I. Witt, u. R. Freytag-Hilf: Zum Mechanismus des Pasteur-Effektes: Bestimmung von ATP, ADP, Orthophosphat und verschiedenen Zwischenprodukten des Kohlenhydratstoffwechsels in lebenden Hefezellen beim Übergang von anaeroben zu aeroben Bedingungen. Biochem. Z. 329, 467 (1958).
HoRiuchi, T., S. Horiuchi and D. Mizuno: A possible negative feedback phenomenon controlling formation of alkaline phosphomonoesterase in Escherichia coli. Nature (Lond.) 183, 1529 (1959).
Horowitz, J., J. J. Saukkonen and E. Chargaff: Effect of 5-fluorouracil On an uracil requiring mutant of Escherichia coli. Biochim. biophys. Acta 29, 222 (1958).
Hurwitz, CH., and C. L. Rosano: Chloramphenicol-sensitive and -insensitive phases of the lethal action of streptomycin. Biochim. biophys. Acta 41, 162 (1960).
Jackson, K. L., and N. Pace: Some permeability properties of isolated rat liver cell mitochondria. J. gen. Physiol. 40, 47 (1957).
Jacob, F., et J. MoNod: Gènes de structure et gènes de régulation dans la biosynthèse des protéines. C.R. Acad. Sci. (Paris) 249, 1282 (1959).
Jacob, F., and E. L. Wollman: Genetic and physical determinations of chromosomal segments in Escherichia coli. Soc. exp. Biol., Sympos. London, p. 75, 1958.
Jacobs, M. H., and D. R. Stewart: The role of carbonic-anhydrase in certain ionic exchanges involving the erythrocyte. J. gen. Physiol. 25, 539 (1942).
Jeener, R.: Biological effects of the incorporation of thiouracil into the ribonucleic acid of tobacco mosaic virus. Biochim. biophys. Acta 23, 351 (1957).
Jeener, R., C. Hamers-Casterman and N. Mairesse: On the inhibition of phage production by 2-thiouracil and 8-azaguanine in an induced lysogenic Bacillus megatherium. Biochim. biophys. Acta 32, 166 (1959).
Johnson, M. J.: The role of aerobic phosphorylation in the Pasteur-effect. Science 94, 200 (1941).
Kempner, E. S., and D. B. Cowie: Metabolic pools and the utilization of aminoacid analogs for protein synthesis. Biochim. biophys. Acta 42, 401 (1960).
Kepes, A.: Etudes cinétiques sur la galactoside-perméase d’Escherichia coli. Biochim. biophys. Acta 40, 70 (1960).
Kepes, A.: Bacterial permeases. 12. Colloquium der Ges. für Physiol. Chemie, Mosbach/Baden, 1961, p. 100. Berlin- Göttingen-Heidelberg: Springer 1961.
Kornberg, A.: Die biologische Synthese von Desoxy-ribonucleinsäure (Dns). Nobel-Vortrag am 11. Dez. 1959. Angew. Chem. 72, 231 (1960).
Krebs, H. A.: The intermediary stages in the biological oxidation of carbohydrate. Adv. Enzymol. 3, 191 (1943).
Krebs, H. A.: Chemical pathways of metabolism, vol. 1, p. 109. New York: Academic Press 1954.
Krebs, H. A.: Die Steuerung der Stoffwechselvorgänge. Dtsch. med. Wschr. 81, 4 (1956).
Krebs, H. A.: The effects of extraneous agents on cell metabolism. In: Ciba Foundation Symposium on Ionizing Radiations and Cell Metabolism (Wolstenholme and O’Connor, eds.), p. 92. London: J. & A. Churchill Ltd. 1956.
Krebs, H. A.: Die Steuerung von Stoffwechselvorgängen. Endeavour 16, 125 (1957).
Krebs, H. A.: Die Steuerung von Stoffwechselvorgängen. Naturw. Rdsch. 11, 79 (1958).
Krebs, H. A., u. H. L. Kornberg: Energy transformation in living matter. Ergebn. Physiol. 49, 212 (1957).
Lacks, S., and R. D. Hotchkiss: Formation of amylomaltase after genetic transformation of Pneumococcus. Biochim. biophys. Acta 45, 155 (1960).
Lamborg, M. R., and P. C. Zamecnik: Amino acid incorporation into protein by extracts of E. coli. Biochim. biophys. Acta 42, 206–211 (1960).
Laser, H., and M. J. Thornley: Stimulation by X-radiation of enzyme induction and growth in Escherichia coli. Proc. roy. Soc. B 150, 539 (1959).
Lederberg, J.: Bacterial protoplasts induced by penicillin. Proc. nat. Acad. Sci. (Wash.) 42, 574 (1956).
Lederberg, J.: Mechanism of action of penicillin. J. Bact. 73, 144 (1957).
Leiner, M.: Die enzymatische Anpassung bei Mikro-Organismen ohne Veränderung des Erbgutes. Ergebn. Mikrobiol. Immun.-Forsch. u. exp. Ther. 31, 35 (1958a).
Leiner, M.: Variable katalytische Aktivität des Fermentes Kohlensäure-Anhydratase (KA) durch Umgebungseinflüsse. Z. Naturforsch. 13b, 242 (1958b).
Leiner, M., u. H. Beck: Von der Hemmbarkeit der katalytischen Aktivität der Kohlensäure-Anhydratase (KA). I. Acta biol. et med. germanica 2, 632 (1959).
Leiner, M., H. Beck u. H. Eckert: Über die Kohlensäure-Dehydratase in den einzelnen Wirbeltierklassen. I. Der Zinkgehalt in den einzelnen Fermenten und die Wirkung des Inhibitors aus dem Schafblut auf die einzelnen Enzyme. Hoppe-Seylers Z. physiol. Chem. 327 (1962).
Lester, G.: Repression and inhibition of indole-synthesizing activity in Neurospora crassa. J. Bact. 82, 215 (1961).
Levin, D. H., and E. Racker: Condensation of arabinose 5-phosphate and phosphoryl enol pyruvate by 2-keto-3-deoxy-8-phosphooctonic acid synthetase. J. biol. Chem. 234, 2532 (1959).
Loomis, W. F.: On the mechanism of action of aureomycin. Science 111, 474 (1950).
Lubin, M., D. H. Kessel, A. Budreau and J. D. Gross: The isolation of bacterial mutants defective in amino acid transport. Biochim. biophys. Acta 42, 535 (1960).
Lynen, F.: Über den aeroben Phosphatbedarf der Hefe. Ein Beitrag zur Kenntnis der Pasteurschen Reaktion. Justus Liebigs Ann. Chem. 546, 120 (1941).
Lynen, F.: Diskussion zum Vortrag H. A. Lardy, Energetic coupling and the regulation of metabolic rates. Proc. 3rd Internat. Congr. Biochem., Brussels 1955, p. 294. New York: Academic Press 1956.
Lynen, F.: Phosphatkreislauf und Pasteur-Effekt. In: Neuere Ergebnisse aus Chemie und Stoffwechsel der Kohlenhydrate. 8. Colloquium der Ges. für Physiol. Chemie, S. 155. Berlin-Göttingen-Heidelberg: Springer 1958.
Lynen, F.: Phosphatkreislauf und Pasteur-Effekt. In: Proc. Intern. Sympos. on Enzyme Chemistry. Tokyo and Kyoto 1957, p. 25. Tokyo: Maruzen 1958.
Lynen, F., G. Hartmann, K. F. Netter and A. Schuegraf: Phosphate turnover and Pasteur effect. Ciba Foundation Sympos. on the regulation of cell metabolism, p. 256. London: J. &. A. Churchill Ltd. 1959.
Lynen, F., u. R. Koenigsberger: Zum Mechanismus der Pasteurschen Reaktion: Der Phosphat Kreislauf in der Hefe und seine Beeinflussung durch 2,4-Dinitrophenol. Über den aeroben Phosphatbedarf der Hefe. VI. Justus Liebigs Ann. Chem. 573, 60 (1951).
Maas, W., and L. Gorini: End-product control for the formation of a biosynthetic enzyme. Fed. Proc. 16, 215 (1957).
Macquillan, A. M., S. Winderman and H. O. Halvorson: The control of enzyme synthesis by glucose and the repressor hypothesis. Biochem. biophys. Res. Commun. 3, 77 (1960).
Magasanik, A. K., and A. Bojarsra: Enzyme induction and repression by glucose in Aerobacter aerogenes. Biochem. biophys. Res. Commun. 2, 77 (1960).
Magasanik, B.: Nutrition of bacteria and fungi. Ann. Rev. Microbiol. 11, 221 (1957).
Magasanik, B.: The metabolic regulation of purine interconversions and of histidine biosynthesis. In: Symposium on the chemical basis of development (Mcelroy and Glass, eds.), p. 485. Baltimore: Johns Hopkins Press 1958.
Magasanik, B., and H. Bowser: The degradation of histidine by Aerobacter aerogenes. J. biol. Chem. 213, 571 (1955).
Magasanik, B, A. K. Magasanik and F. C. Neidhardt: Regulation of growth and composition of the bacterial cell. Ciba Foundation Symposium on the regulation of cell metabolism, p. 334. London: J. &. A. Churchill Ltd. 1959.
Magasanik, B., F. C. Neidhardt and A. P. Levin: Metabolic regulation of enzyme biosynthesis in bacteria. In: Physiological adaptation (edit. C. L. Prosser), pp. 159–166. Washington D. C.: American Physiological Society 1958.
Mager, J.: Chloramphenicol and chlortetracycline inhibition of amino acid incorporation into proteins in a cell-free system from Tetrahymena pyriformis. Biochim. biophys. Acta 38, 150 (1960).
Mager, J., and B. Magasanik: Guanosine 5’-phosphate reductase and its role in interconversion of purine nucleotides. J. biol. Chem. 235, 1474 (1960).
Mandel, H. G.: Incorporation of 8-azaguanine and growth inhibition in Bacillus cereus. J. biol. Chem. 225, 137 (1957).
Mandel, H. G., and R. Markham: The effects of 8-azaguanine on the biosynthesis of ribonucleic acid in Bacillus cereus. Biochem. J. 69, 297 (1957).
Mandel, H. G., G. J. Sugerman and R. A. Apter: Fractionation studies of Bacillus cereus containing 8-azaguanine. J. biol. Chem. 225, 151 (1957).
Mandelstam, J.: Turnover of protein in starved bacteria and its relationship to the induced synthesis of enzyme. Nature (Lond.) 179, 1179 (1957).
Marsh, C. L., and G. W. Kelley: Studies in helminth enzymology. I. Inorganic pyrophosphatase activity in some helminth parasites of domestic animals. Exp. Parasit. 7, 366 (1958).
Marsh, C. L., and G. W. Kelley: Studies in helminth enzymology. II. Properties of an inorganic pyrophosphatase from Ascaridia galli, a nematode parasite of chickens. Exp. Parasit. 8, 274 (1959).
Marshax, A.: Processes co-ordinating intracellular activity. Soc. Exp. Biol., Symposium London 205 (1958).
Martin, G., et G. Legrand: Recherches sur les facteurs de production de la laccase par le mycélium d’Agaricus campestris. IV. Influence de la teneur en manganèse du milieu de culture. Bull. Soc. Chim biol. (Paris) 41, 1463 (1959).
Matthews, R. E. F.: Incorporation of unnatural bases into nucleic acids. Proc. 3rd internat. Congr. Biochem, Brussels 1955, p. 63. New York: Academic Press 1956.
Mclaren, A. D.: Enzyme action in structurally restricted systems. Enzymologia 21, 356 (1960).
Melnykovych, G., and K. R. Johansson: Effects of chlortetracycline on the stability of arginine decarboxylase in Escherichia coli. J. Bact. 77, 638 (1959).
Melnykovych, G., and E. E. Snell: Nutritional requirements for the formation of arginine decarboxylase in Escherichia coli. J. Bact. 76, 518 (1958).
Mentzer, C., P. Meunier and L. Molho-Lacroix: Faits de synergie et d’antagonism entre la chloromycetine et divers amino-acides vis-à-vis de cultures d’E. coli. C.R. Acad. Sei. (Paris) 230, 241 (1950).
Meyerhof, O.: Über die Kinetik der umkehrbaren Reaktionen zwischen Hexodiphosphorsäure und Dioxyacetonphosphorsäure. Biochem. Z. 277, 77 (1935).
Miller, C. P., and M. Bohnhoff: Development of streptomycin-resistant variants of Meningococcus. Science 105, 620 (1947).
Miller, D M: The osmotic pump theorie of selective transport. Biochim. biophys. Acta 37, 448 (1960).
Minagawa, T.: Studies on the adaptation of yeast to copper. Xix Effect of copper on cytochrome components of yeast. Exp. Cell. Res. 14, 333 (1958).
Mitchell, P. D., and J. Moyle: Relationships between cell growth, surface properties and nucleic acid production in normal and penicillin-treated Micrococcus pyogenes. J. gen. Microbiol. 5, 421 (1951).
Mokrasch, L. C., and S. Grisolla: Contribution of hydrouracil and its derivatives to pyri- midine biosynthesis. II. Mechanism studies. Biochim. biophys. Acta 34, 165 (1959).
Monod, J.: Information, induction, repression dans la biosynthèse d’un enzyme. 10. Colloquium der Ges. für Physiol. Chemie, Mosbach/Baden, „Dynamik des Eiweißes“, p. 120. Berlin- Göttingen-Heidelberg: Springer 1960.
Monod, J., et G. Cohen-Bazire: L’effet inhibiteur spécifique des ß-galactosides dans la biosynthèse “constitutive” de la ß-galactosidase chez E. coli. C. R. Acad. Sci. (Paris) 236, 417 (1953).
Monod, J., et G. Cohen-Bazire: L’effet d’inhibition spécifique dans la biosynthèse de la tryptophane-desmase chez Aerobacter aerogenes. C.R. Acad. Sci. (Paris) 236, 530 (1953).
Morton, A. G., A. G. F. Dickerson and D. J. F. England: Changes in enzyme activity of fungi during nitrogen starvation. J. exp. Bot. 11, 116 (1960).
Munier, R., et G. N. Cohen: Incorporation d’analogues structuraux d’aminoacides dans les protéines bactériennes. Biochim. biophys. Acta 21, 592 (1956).
Munier, R., et G. N. Cohen: Incorporation d’analogues structuraux d’aminoacides dans les protéines bactériennes au cours de leur synthèse in vivo. Biochim. biophys. Acta 31, 378 (1959).
Myrback, K.: Die Hemmung der Hefeinvertase (Saccharase) durch Metallionen. 2. Mitt. Die Wirkung von Ag+, Cu+, Cd2}, Zn2+ und deren Komplexbildung mit Acetationen. Ark. Kemi (Stockh.) 8, 393 (1956).
Neidhardt, F. C.: Mutant of Aerobacter aerogenes lacking glucose repression. J. Bact. 80, 536 (1960).
Neidhardt, F. C., and F. Gros: Metabolic instability of the ribonucleic acid synthesized by Escherichia coli in the presence of Chloromycetin. Biochim. biophys. Acta 25, 513 (1957).
Neidhardt, F. C., and B. Magasanik: The effect of glucose on the induced biosynthesis of bacterial enzymes in the presence and absence of inducing agents. Biochim. biophys. Acta 21, 324 (1956).
Neidhardt, F. C., and B. Magasanik: Inhibitory effect of glucose on enzyme formation. Nature (Lond.) 178, 801 (1956).
Neidhardt, F. C., and B. Magasanik: Reversal of the glucose inhibition of histidinase biosynthesis in Aerobacter aerogenes. J. Bact. 73, 253 (1957).
Neidhardt, F. C., and B. Magasanik: Effect of mixtures of substrates on the biosynthesis of inducible enzymes in Aerobacter aerogenes. J. Bact. 73, 260 (1957).
Netter, H.: Mögliche Mechanismen und Modelle für aktive Transportvorgänge. 12. Colloquium der Ges. für Physiol. Chemie, Mosbach/Baden, 1961, p. 15 Berlin-Göttingen-Heidelberg: Springer 1961.
Nomura, M., J. Hosoda, B. Maruo and S. Akabori: Studies on amylase formation by Bacillus subtilis. II. Effect of amino acid analogues on amylase formation by Bacillus subtilis; an apparent competition between amylase formation and normal cellular protein synthesis. J. Biochem. (Tokyo) 43, 841 (1956).
Northrop, J. H.: Adaptation of Bacillus megatheriune to terramycin (Oxytetracycline). J. gen. Physiol. 40, 547 (1957).
Novicx, A., and L. Szilard: Description of the Chemostat. Science 112, 715 (1950).
Novicx, A., and L. Szilard: Dynamics of growth processes, p. 21. Princeton: University Press 1954.
Ochoa, S.: Enzymatic synthesis of polyribonucleotides. (An introduction to the two following lectures). Proc. 4th internat. Congr. Biochem., Vienna 1958, IX, p. 133, 1959.
Ochoa, S.: Die enzymatische Synthese von Ribonucleinsäure (Rns). Nobel-Vortrag am 11. Dez. 1959. Angew. Chem. 72, 225 (1960).
Osawa, S.: The nucleotide composition of ribonucleic acids from subcellular components of yeast. E. coli and rat liver, with special reference to the occurence of pseudouridylic acid in soluble ribonucleic acid. Biochim. biophys. Acta 42, 244 (1960).
Palmer, I. S., and M. F. Mallette: The effect of exogenous sources on the synthesis of ß-galactosidase in resting-cell suspensions of Escherichia coli. J. gen. Physiol. 45, 229 (1961).
Pardee, A. B.: Effect of energy supply on enzyme induction by pyrimidine requiring mutants of Escherichia coli. J. Bact. 69, 233 (1955).
Pardee, A. B.: An inducible mechanism for accumulation of melibiose in Escherichia coli. J. Bact. 73, 376 (1957).
Pardee, A. B.: Mechanisms for control of enzyme synthesis and enzyme activity in bacteria. Ciba Foundation Symposium on the regulation of cell metabolism, p. 295. London: J. &. A. Churchill Ltd. 1959.
Pardee, A. B.: The control of enzyme activity. In: The enzymes (Boyer, Lardy and MyrbÄCK, eds.), 2nd edit., vol. 1, p. 681. New York: Academic Press 1959.
Pardee, A. B., F. Jacob et J. Monod: Sur l’expression et le rôle des allèles “inductible” et “constitutif” dans la synthèse de la ß-galactosidase chez des zygotes d’Escherichia coli. C. R. Acad. Sci. (Paris) 246, 3125 (1958).
Pardee, A. B.: The genetic control and cytoplasmic expression of “inductibility” in the synthesis of ß-galaetosidase by E. coli. J. molec. Biol. 1, 165 (1959).
Pardee, A. B., K. Paigen and L. S. Prestidge: A study of the ribonucleic acid of normal and chloromycetin-inhibited bacteria by zone electrophoresis. Biochim. biophys. Acta 23, 162 (1957).
Pardee, A. B., and L. S. Prestidge: Effects of azatryptophan on bacterial enzymes and bacteriophage. Biochim. biophys. Acta 27, 330 (1958).
Pardee, A. B., and L. S. Prestidge: On the nature of the repressor of ß-galactosidase synthesis in E. coli. Biochim biophys. Acta 36, 545 (1959).
Pardee, A. B., V. G. Shore and L. S. Prestidge: Incorporation of azatryptophan into proteins of bacteria and bacteriophage. Biochim. biophys. Acta 21, 406 (1956).
Park, J. T.: Selective inhibition of bacterial cell-wall synthesis: its possible applications in chemotherapy. 8th Sympos. Soc. gen. Microbiol., London 1958: The strategy of chemotherapy, p. 49. Cambridge: Cambridge Univ. Press 1958.
Park, J. T., and M. J. Johnson: Accumulation of labile phosphate in Staphylococcus aureus grown in the presence of penicillin. J. biol. Chem. 179, 595 (1949).
Park, J. T., and J. L. Strominger: Mode of action of penicillin Biochemical basis for the mechanism of action of penicillin and for its selective toxity. Science 125, 99 (1957).
Parr, C. W.: Inhibition of phosphoglucose isomerase. Nature (Lond.) 78, 1401 (1956).
Parr, C. W.: Competitive inhibitors of phosphoglucose isomerase. Biochem. J. 65, 34 (1957).
Passow, H.: Zusammenwirken von Membranstruktur und Zellstoffwechsel bei der Regulierung der Ionenpermeabilität roter Blutkörperchen. 12. Colloquium der Ges. für Physiol. Chemie, Mosbach/Baden, 1961, p. 54. Berlin-Göttingen-Heidelberg: Springer 1961.
Polglase, W. J.: The effect of dihydrostreptomycin on the formation of ß-galactosidase by Escherichia coli. Canad. J. Biochem. 34, 554 (1956).
Polglase, W. J., S. Peretz and S. M. Roote: Adaptive enzyme formation by dihydrostreptomycindependent E. coli. Canad. J. Biochem. 34, 558 (1956).
Porter, K. R., and G. E. Palade: Studies on the endoplasmic reticulum. Iii. Its form and distribution in striated muscle cells. J. biophys. biochem. Cytol. 3, 269 (1957).
Quayle, J. R., and D. B. Keech: Carbon dioxide and formate utilization by formate-grown Pseudomonas oxylaticus. Biochim. biophys. Acta 29, 223 (1958).
Quayle, J. R., and D. B. Keech: Carboxydismutase activity in formate-and oxalate-grown Pseudomonas oxalaticus (Strain 0 X 1). Biochim biophys. Acta 31, 587 (1959).
Raacke, I. D.: Studies on protein synthesis with ribonucleoprotein particles from pea seedlings. Biochim. biophys. Acta 34, 1 (1959).
Racker, E., and R. Wu: Limiting factors in glycolysis of ascites tumor cells and the Pasteur effect. Ciba Foundation Sympos. on the regulation of cell metabolism, p. 205. London: J. &. A. Churchill Ltd. 1959.
Reichard, P., and G. Hanshoff: Aspartate carbamyl transferase from E. coli. Acta them. stand. 10, 548 (1956).
Reiner, J. M.: Induced enzyme synthesis in cell-free preparations of E. coli. J. Bact. 79, 157 (1960).
Reiner, J. M.: Macromolecular synthesis in cell-free preparations from E. coli. J. Bact. 79, 166 (1960).
Richmond, M. H.: Formation of a lytic enzyme by a strain of Bacillus subtilis. Biochim. biophys. Acta 33, 78 (1959).
Richmond, M. H.: Properties of a lytic enzyme produced by a strain of Bacillus subtilis. Biochim. biophys. Acta 33, 92 (1959).
Richmond, M. H.: Effect of inhibitors on lytic enzyme synthesis by Bacillus subtilis R. Biochim. biophys. Acta 34, 325 (1959).
Rickenberg, H. V., G. N. Cohen, G. Buttin et J. Monod: La galactoside-perméase d’Eecherichia coli. Ann. Inst. Pasteur Paris 91, 829 (1956).
Rickenberg, H. V., and G. Lester: The preferential synthesis of ß-galactosidase in Escherichia coli. J. gen. Microbiol. 13, 279 (1955).
Rogers, P., and G. D. Novelli: Formation of ornithine transcarbamylase in cells and protoplasts of E. coli. Biochim. biophys. Acta 33, 423 (1959).
Rogers, P., and G. D. Novelli: Cell free synthesis of ornithine transcarbamylase. Biochim. biophys. Acta 44, 298 (1960).
Sachs, H., and H. Waelsch: The effect of pyrophosphate on amino acid incorporation into rat liver microsomes. Biochim. biophys. Acta 21, 188 (1956).
Sacks, J.: Mechanism of phosphate transfer across cell membranes. Cold Spr. Harb. Symp. quant. Biol. 18, 180 (1948).
Saz, A. K., and J. Marmur: The inhibition of organic nitro-reductase by aureomycin in cell-free extracts. Proc. Soc. exp. Biol. (N.Y.) 82, 783 (1953).
Saz, A. K., and L. M. Martinez: Enzymatic basis of resistance to aureomycin. 1. Differences between flavoprotein nitro reductase of sensitive and resistant Escherichia coli. J. biol. Chem. 223, 285 (1956).
Saz, A. K., and R. B. Slie: The inhibition of organic nitro reductase by aureomycin in cell-free extracts. 2. Cofactor requirements for the nitro reductase enzyme complex. Arch. Biochem. 51, 5 (1954).
Saz, A. K., and R. B. Slie: Reversal of aureomycin inhibition of bacterial cell-free nitro reductase by manganese. J. biol. Chem. 210, 407 (1954).
Schanberg, S., and N. J. Giarman: Uptake of 5-hydroxytryptophan by rat’s brain. Biochim. biophys. Acta 41, 556 (1960).
Schneider, J. H., and V. R. Potter: Nucleotide metabolism. Viii. Heterogenous labelling in ribonucleic acid of rat liver. J. biol. Chem. 233, 154 (1958).
Schwartzman, G.: On the nature of refractoriness of certain gram-negative bacilli to penicillin. Science 101, 276 (1945).
Sharon, N., and F. Lipmann: Reactivity of analogs with pancreatic tryptophan-activating enzyme. Arch. Biochem. 69, 219 (1957).
Sheinin, R., and B. F. Crocker: The induced concurrent formation of a-galactosidase and ß-galactosidase in Escherichia coli B. Canad. J. Biochem. 39, 63 (1961).
Sheinin, R., and K. Mc Quillen: Effect of penicillin on induced enzyme formation in normal cells and spherical forms of E. coli. Biochim. biophys. Acta 31, 72 (1959).
Shiraki, S.: Studies on the adaptive enzyme system of Mycobacterium avium. Nagoya J. med. Sci. 22, 315 (1959).
Siekevitz, P.: On the meaning of intracellular structure for metabolic regulation. Ciba Foundation Sympos. on the regulation of cell metabolism, p. 17. London: J. & A. Churchill Ltd. 1959.
Silberman, H., and J. B. Wyngaarden: Mercaptopurine as substrate and inhibitor of xanthine oxidase. Biochim. biophys. Acta 47, 178 (1961).
Skoda, J., J. Kara, Z. Sormova and F. Sorm: Inhibition of Escherichia coli polynueleotide phosphorylase by 6-azauridine diphosphate. Biochim. biophys. Acta 33, 579 (1959).
Smith, G. N.: The possible modes of action of chlorormycetin. Bact. Rev. 17, 19 (1953).
Smith, G. N., C. S. Worrel and A. L. Swanson: Inhibition of bacterial esterases by chloramphenicol (chloromycetin). J. Bact. 58, 803 (1949).
Smith, J. D., and R. E. F. Matthews: The metabolism of 8-azapurines. Biochem. J. 66, 323 (1957).
Snodgrass, P. J., B. L. Vallee and F. L. Hoch: Effects of silver and mercurials on yeast alcohol dehydrogenase. J. biol. Chem. 235, 504 (1960).
Spiegelman, S., H. O. Halvorson and R. Ben-Ishai: Free amino acids and the enzyme-forming mechanism. Symposium on amino acid metabolism (McElroy and Glass, eds.), p. 124. Baltimore: Johns Hopkins Press 1955.
Stadtman, E. R., G. N. Cohen, G. Le Bras and H. Robichon-Szulmajster: Feed-back inhibition and repression of aspartokinase activity in Escherichia coli and Saccharomyces cerevisiae. J. biol. Chem. 236, 2033 (1961).
Stein, E. A., and E. H. Fischer: Bacillus subtilis a-amylase, a zinc-protein complex. Biochim. biophys. Acta 39, 287 (1960).
Stoeber, F.: Sur la biosynthèse induite de la ß-glucuronidase chez E. coli. C. R. Acad. Sci. (Paris) 244, 950 (1957).
Stoeber, F.: Sur la ß-glucuronide-perméase d’Escherichia coli. C. R. Acad. Sci. (Paris) 244, 1091 (1957).
Stouthamer, A. H.: Glucose and galaktose metabolism in Gluconobacter liquefaciens. Biochim. biophys. Acta 48, 484 (1961).
Strange, R. E.: Induced enzyme synthesis in aqueous suspensions of starved stationary phase Aerobacler aerogenes. Nature (Loud.) 191, 1272 (1961).
Straub, F. B., and A. Ullmann: On the mechanism of amylase synthesis. Biochim. biophys. Acta 23, 665 (1957).
Straus, D. B., and E. Goldwasser: A new synthesis of (32P) uridine 5’-phosphate. Biochim. biophys. Acta 47, 186 (1961).
Suzuxl, K., F. Sawada and Y. Iwama: Effects of chloramphenicol on Rna synthesis in Escherichia coli irradiated with ultraviolet light. Biochim. biophys. Acta 37, 369 (1960).
Tabor, H., and A. H. Mehler: Histidase and urocanase. In: Methods in enzymology (Colowick and Kaplan), vol. II, p. 228. New York: Academic Press, 1955.
Timm, F.: Zur Entstehung der Penicillinresistenz. Naturwissenschaften 44, 266 (1957).
Tomasz, A., and E. Borek: The mechanism of bacterial fragility by 5-fluorouracil: The accumulation of cell wall precursors. Proc. nat. Acad. Sci. (Wash.) 46, 324 (1960).
Torriani, A.: Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim. biophys. Acta 38, 460 (1960).
Touzi, A.: Recherches sur le metabolisme de Colletotrichum oligochaetumCav. et de Colletotrichum lindemuthianum (Sacc. et Magn.). Bri. et Cay. II. Synthèse d’un enzyme d’adaptation: la guanidinase. C.R. Acad. Sci. (Paris) 245, 2077 (1957).
Umbarger, H. E.: Some observations on the biosynthetic pathway of isoleucine. In: Amino acid metabolism (Mcelroy and Glass, eds.), p. 442. Baltimore: Johns Hopkins Press 1955.
Umbarger, H. E.: Evidence for a negative feedback mechanism in the biosynthesis of isoleucine. Science 123, 848 (1956).
Umbarger, H. E., and B. Brown: Isoleucine and valine metabolism in E. coli. Vii. A negative feedback mechanism controlling isoleucine biosynthesis. J. biol. Chem. 233, 415 (1958).
Ussing, H. H.: Experimental evidence and biological significance of active transport. 12. Colloquium der Ges. für Physiol. Chemie, Mosbach/Baden, 1961, p. 1 Berlin-GöttingenHeidelberg: Springer 1961
Vallee, B. L., J. A. Rupley, L. CoOmbs and H. Neurath: The role of zinc in carboxypeptidase. J. biol. Chem. 235, 64 (1960).
Vaughan, M., and D. Steinberg: Incorporation of p-fluorophenyl-alanine into crystalline proteins. Fed. Proc. 17, 328 (1958).
Vaughan, M., and D. Steinberg: Incorporation of amino acid analogues into crystalline proteins. Proc. 4th Internat. Congr. Biochem., Vienna, vol. 8, p. 234. New York: Pergamon Press 1959.
Vaughan, M., and D. Steinberg: Biosynthetic incorporation of flurorophenylalanine into crystalline proteins. Biochim. biophys. Acta 40, 230 (1960).
Vogel, H. J.: Repression and induction as control mechanisms of enzyme biogenesis: The “adaptive” formation of acetylornithinase. Sympos. Chem. Basis of Heredity (Mcelroy and Glass, eds.), p. 276. Baltimore: Johns Hopkins Press (1957a).
Vogel, H. J.: Repressed and induced enzyme formation: a unified hypothesis. Proc. nat. Acad. Sci. (Wash.) 43, 491 (1957b).
Vogel, H. J.: A “pace-setting” phenomenon in derepressed enzyme formation. Biochem. biophys. Res. Commun. 3, 373 (1960).
Vogel, H., P. H. Abelson and E. T. Bolton: On ornithin and prolin synthesis in Escherichia coli. Biochim. biophys. Acta 11, 584 (1953).
Vogel, H., and D. M. Bonner: On the glutamate-proline-ornithine interrelation in Neurospora crassa. Proc. nat. Acad. Sci. (Wash.) 40, 688 (1954).
Vogel, H., and D. M. Bonner: Acetylornithinase of Escherichia coli: partial purification and some properties. J. biol. Chem. 218, 97 (1956).
Vogel, H., and D. M. Bonner: Handbuch der Pflanzenphysiologie, Bd. Xii (Hrsg. Ruhland), vol. 11, Kap. II. Berlin-Göttingen-Heidelberg: Springer 1960.
Vogel, H., and B. D. Davis: Adaptive phenomena in a biosynthetic pathway. Fed. Proc. 11, 485 (1952).
Wacker, A., A. Trebst u. FR. Weygand: 5-Bromuracildesoxyribosid, ein Wuchsstoff für Lb. leichmannii und Lb. acidophilus R 26. Z. Naturforsch. 11b, 7 (1956).
Wainwright, S. D.: On the development of increased tryptophan synthetase enzyme activity by cell-free extracts of Neurospora crassa. Canad. J. Biochem. 37, 1417 (1959).
Wainwright, S. D., and D. M. Bonner: On the induced synthesis of an enzyme required for biosynthesis of an essential metabolite: induced kynureninase synthesis in Neurospora crassa. Canad. J. Biochem. 37, 741 (1959).
Wainwright, S. D., and M. R. Pollocx: Enzyme adaptation in bacteria: fate of nitratase in nitrate-adapted cells grown in the absence of substrate. Brit. J. exp. Path. 30, 190 (1949).
Wallenfels, K., O. P. Malhotra u. D. Dabich: Untersuchungen über milchzuckerspaltende Enzyme Viii. Der Einfluß des Kationen-Milieus auf die Aktivität der ß-Galaktosidase von E. coli ML 309. Biochem. Z. 333, 377 (1960).
Wallenfels, K., u. H. Sund: Über den Mechanismus der Wasserstoffübertragung mit Pyridinnucleotiden. I. Freie SH-Gruppen und Aktivität bei Alkoholdehydrogenase aus Hefe. Biochem. Z. 329, 17 (1957).
Watanabe, Y., and K. SH Mura: Biosynthesis of threonine from homoserine. J. Biochem. (Tokyo) 42, 181 (1955).
Wilbrandt, W.: Zuckertransporte. 12. Colloquium der Ges. für Physiol. Chemie, Mosbach/ Baden, 1961, p. 112. Berlin-Göttingen-Heidelberg: Springer 1961.
Williams, R. J. P., F. L. Hoch and B. L. Vallee: The role of zinc in alcohol dehydrogenases. Iii. The kinetics of a time-dependent inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline. J. biol. Chem. 232, 465 (1958).
Wisseman, C. L., J. E. Smadel, F. E. Hahn and H. E. Hopps: Mode of action of chloramphenicol. I. Action of chloramphenicol on assimilation of ammonia and on synthesis of proteins and nucleic acids in E. coli. J. Bact. 67, 662 (1954).
Wolfe, A. D., and F. E. Hahn: Discrepancy between thienylalanine activation and protein synthesis in bacteria. Biochim. biophys. Acta 41, 545 (1960).
Woolley, D. W.: A study of non-competitive antagonism with chloromycetin and related analogues of phenylalanine. J. biol. Chem. 185, 293 (1950).
Woolley, D. W.: Selective toxicity of 1,2-dichloro-4,5-diamino-benzene: its relation to requirements for riboflavin and vitamin B12. J. exp. Med. 93, 13 (1951).
Woolley, D. W.: The designing of antimetabolites. 8th Sympos. Soc. Gen. Microbiol., London 1958: The strategy of chemotherapy, p. 139. Cambridge: Cambridge Univ. Press 1958.
Woolley, D. W., and D. W. Schaffner: Effect of analogs of dimethyl-diaminobenzene on various strains of transplanted mammary cancers of mice. Cancer Res. 14, 802 (1954).
Wormser, E. H., and A. B. Pardee: Regulation of threonine biosynthesis in E. coli. Arch. Biochem. 78, 416 (1958).
Yanofsky, C., and M. Racrmeler: The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim. biophys. Acta 28, 640 (1958).
Yates, R. A., and A. B. Pardee: Pyrimidine biosynthesis in Escherichia coli. J. biol. Chem. 221, 743 (1956).
Yates, R. A., and A. B. Pardee: Control of pyrimidine biosynthesis in E. coli by a feed-back mechanism. J. biol. Chem. 221, 757 (1956).
Yates, R. A., and A. B. Pardee: Control by uracil of formation of enzymes required for orotate synthesis. J. biol. Chem. 227, 677 (1957).
Yeas, M., and G. Brawerman: Interrelations between nucleic acid and protein biosynthesis in microorganisms. Arch. Biochem. 68, 118 (1957).
Yoshida, A.: Studies on the mechanism of protein synthesis: bacterial a-amylase containing ethionine. Biochim. biophys. Acta 29, 213 (1958).
Yoshida, A.: Studies on the mechanism of protein synthesis: incorporation of p-fluorophenylalanine into a-amylase of Bacillus subtilis. Biochim. biophys. Acta 41, 98 (1960).
Yoshida, A., and M. Yamasaki: Studies on the mechanism of protein synthesis: incorporation of ethionine into a-amylase of Bacillus subtilis. Biochim. biophys. Acta 34, 158 (1959).
Yoshiikawa, H., and B. Maruo: Stimulation of amylase formation by an amine from Bacillus subtilis. Biochim. biophys. Acta 45, 270 (1960).
Zador, ST.: Redox potential studies on the action-mechanism of antibiotics. Jap. J. Pharmacol. 9, 75 (1959).
Zubay, G.: The interaction of nucleic acid with Mg-ions. Biochim. biophys. Acta 32, 233 (1959).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1962 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Leiner, M. (1962). Über die Stoffwechselregulation in der Zelle. In: Henle, W., Kikuth, W., Meyer, K.F., Nauck, E.G., Tomcsik, J. (eds) Ergebnisse der Mikrobiologie Immunitätsforschung und Experimentellen Therapie. Current Topics in Microbiology and Immunology, vol 35. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-42624-1_4
Download citation
DOI: https://doi.org/10.1007/978-3-662-42624-1_4
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-02812-3
Online ISBN: 978-3-662-42624-1
eBook Packages: Springer Book Archive