L-Asparaginase: Basic Aspects

  • M. K. PattersonJr.
Part of the Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology book series (HEP, volume 38 / 2)

Abstract

L-Asparaginase (L-asparagine amidohydrolase, E.C.3.5.1.1) catalyzes the hydrolysis of L-asparagine to yield L-aspartic acid and ammonia. The enzyme was first reported by Lang (1904), who demonstrated its activity in various beef tissues. Confirmatory observations with tissues from horse and pig were reported a few years later by Von Furth and Friedmann (1910). The observation most pertinent to the current discussion, however, was that of Clementi (1921, 1922), who found that of numerous blood sera tested only that of the guinea pig showed L-asparaginase activity.

Keywords

Amide Tuberculosis Sarcoma Methotrexate Aspergillus 

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References

  1. Abdou, N. I., Richter, M.: The role of bone marrow in the immune response. Advanc. Immunol. 12, 201–270 (1970).Google Scholar
  2. Adamson, R. H., Fabro, S.: Antitumor activity and other biologic properties of L-asparaginase (NSC-109229) — A review. Cancer Chemother. Rep. 52, 617–626 (1968a).PubMedGoogle Scholar
  3. Adamson, R. H., Fabro, S.: Embryotoxic effect of L-asparaginase. Nature (Lond.) 218, 1164–1165 (1968b).Google Scholar
  4. Adamson, R. H., Fabro, S., Hahn, M. A., Creech, C. E., Whang-Peng, J.: Evaluation of the embryotoxic activity of L-asparaginase. Arch. int. Pharmacodyn. 186, 310–320 (1970).PubMedGoogle Scholar
  5. Allison, J. P., Mandy, W. J., Kitto, G. B.: The substrate specificity of L-asparaginase from Alcaligenes eutrophus. FEBS Let. 14, 107–108 (1971).Google Scholar
  6. Altenbern, R. A., Housewright, R. D.: Stereospecific asparaginases in smooth Brucella abortus strain 19. Arch. Biochem. Biophys. 49, 130–137 (1954).PubMedGoogle Scholar
  7. Arens, A., Rauenbuch, E., Irion, E., Wagner, O., Bauer, K., Kaufmann,W.: Isolation and properties of L-asparaginase from Escherichia coli. Hoppe-Seylers Z. Physiol. Chem. 351, 197–212 (1970).Google Scholar
  8. Arfin, S. M.: Asparagine synthesis in the chick embryo liver. Biochim. biophys. Acta (Amst.) 136, 233–244 (1967).Google Scholar
  9. Astaldi, G., Burgio, G. R., Biscatti, G., Astaldi, A., Jr., Ferfoglia, L.: L-Asparaginase and blastogenesis. Lancet II, 643–644 (1969b).Google Scholar
  10. Astaldi, G., Burgio, G. R., KRC, J., Genova, R., Astaldi, A., Jr.: L-Asparaginase and blastogenesis. Lancet I, 423 (1969 a). Astaldi, G., Micu, D., Astaldi, A., Jr., Burgio, G. R., KRC, I.: Further investigations on L-asparaginase and immune reactions. Colloq. Intern. Centre Natl. Rech. Scien. (Paris) 197, 205–219 (1971).Google Scholar
  11. Astaldi, G., Micu, D., Astaldi, A., Jr., Burgio, G. R.: Immunosuppressive action of L-as-paraginase. Lancet II, 1357 (1969 c).Google Scholar
  12. Astaldi, G., Micu, D., Astaldi, A., Jr., Burgio, G. R.: Immunological effect of E. coli L-as-paraginase. Blut 21, 273–282 (1970).Google Scholar
  13. Bauer, K.: Zur Biochemie der Asparaginase. Med. Klin. 64, 9–12 (1969).PubMedGoogle Scholar
  14. Becker, F. F., Baserga, R., Broome, J. D.: Effect of L-asparaginase on DNA synthesis in regenerating liver and in other dividing tissues. Cancer Res. 30, 133–137 (1970).PubMedGoogle Scholar
  15. Becker, F. F., Broome, J. D.: L-Asparaginase: inhibition of early mitosis in regenerating rat liver. Science 156, 1602–1603 (1967).PubMedGoogle Scholar
  16. Becker, F. F., Broome, J. D.: L-Asparaginase: inhibition of endogenous RNA polymerase activity in regenerating liver. Arch. Biochem. Biophys. 130, 332–336 (1969).PubMedGoogle Scholar
  17. Begemann, H., Kaboth, W., Fink, U., Theml, H.: Clinical studies on treatment of auto- immunological disorders with L-asparaginase. Colloq. Intern. Centre Natl. Rech. Scien. (Paris) 197, 195–198 (1971).Google Scholar
  18. Benezra, D., Hochman, A., Pitaro, R.: L-Asparaginase and blastogenesis. Lancet I, 1235–1236 (1970).Google Scholar
  19. Benson, J. V., Jr., Gordon, M. J., Patterson, J. A.: Accelerated chromatographic analysis of amino acids in physiological fluids containing glutamine and asparagine. Anal. Biochem. 18, 228–240 (1967).Google Scholar
  20. Berenbaum, M. C.: Immunosuppression by L-asparaginase. Nature (Lond.) 225, 550–552 (1970).Google Scholar
  21. Berenbaum, M. C., Bondurant, S.: Effect of L-asparaginase on germinal centre haemolysin. Nature (Lond.) 231, 318–319 (1971).Google Scholar
  22. Berenbaum, M. C., Ginsburg, H., Gilbert, D. M.: Effects of L-asparaginase on lymphocyte- target cell reactions in vitro. Nature (Lond.) 227, 1147–1148 (1970).Google Scholar
  23. Bertelli, A., Donati, L., Tbabucchi, E., Jr.: Prolonged survival of allo- and xeno-grafts of skin by means of an antitumoral compound: the L-asparaginase. Arch. ital. pat. 11, 475–479 (1968).Google Scholar
  24. Bilimoria, M. H.: Conditions for the production of L-asparaginase 2 by coliform bacteria. Appl. Microbiol. 18, 1025–1030 (1969).PubMedGoogle Scholar
  25. Bilimoria, M. H., Nisbet, M. A.: The effect of acrolein on L-asparaginase 2 from Escherichia coli. Proc. Soc. exp. Biol. (N.Y.) 130, 698–700 (1971).Google Scholar
  26. Boch, D.: Les conditions d’action de l’asparaginase de l’Aspergillus niger. C.R. Soc. Biol. (Paris) 187, 955–956 (1928).Google Scholar
  27. Bonetti, E., Abbondanza, A., Cobte, E. D., Stibpe, F.: The regulation of L-asparaginase activity in rats and mice. Biochem. J. 115, 597–601 (1969).PubMedGoogle Scholar
  28. Bosmann, H. B.: Asparaginase action: Inhibition of protein synthesis in rat liver mitochondria and microsomes and brain mitochondria and inhibition of glycoprotein synthesis in liver and brain mitochondria by asparaginase. Life Sci. 9, 851–859 (1970).Google Scholar
  29. Bosmann, H. B., Kessel, D.: inhibition of glycoprotein synthesis in L5178Y mouse leukaemic cells by L-asparaginase in vitro. Nature (Lond.) 226, 850 — 851 (1970).Google Scholar
  30. Boyd, J. W., Phillips, A. W.: Purification and properties of L-asparaginase from Serratia marcescens. J. Bact. 106, 578 — 587 (1971).PubMedGoogle Scholar
  31. Boyse, E. A., Old, L. J., Campbell, H. A., Mashbubn, L. T.: Suppression of murine leukemias by L-asparaginase. J. exp. Med. 125, 17–31 (1967).PubMedGoogle Scholar
  32. Boyse, E. A., Old, L. J., Stockert, E.: Inhibitory effect of guinea pig serum on a number of new leukaemias in mice. Nature (Lond.) 198, 800 (1963).Google Scholar
  33. Brambilla, G., Parodi, S., Cavanna, M., Cabaceni, C. E., Baldini, L.: The immunodepressive activity of Escherichia coli L-asparaginase in some transplantation systems. Cancer Res. 30, 2665–2670 (1970).PubMedGoogle Scholar
  34. Breuer, L. H., Warner, R. G., Benton, D. A., Loosli, J. K.: Dietary requirement for aspara- gine and its metabolism in rats. J. Nutr. 88, 143–150 (1966).PubMedGoogle Scholar
  35. Broome, J. D.: Evidence that the L-asparaginase activity of guinea pig serum is responsible for its antilymphoma effects. Nature (Lond.) 191, 1114–1115 (1961).Google Scholar
  36. Broome, J. D.: Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. I. Properties of the L-asparaginase of guinea pig serum in relation to those of the antilymphoma substance. J. exp. Med. 118, 99–120 (1963 a).Google Scholar
  37. Broome, J. D.: Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma 6C3HED cells cultured in a medium devoid of L-asparagine lose their susceptibility to the effects of guinea pig serum in vivo. J. exp. Med. 118, 121–148 (1963b).PubMedGoogle Scholar
  38. Broome, J. D.: Antilymphoma activity of L-asparaginase in vivo: clearance rates of enzyme preparations from guinea pig serum and yeast in relation to their effect on tumor growth. J. nat. Cancer Inst. 35, 967–974 (1965).PubMedGoogle Scholar
  39. Broome, J. D.: A method for estimating free asparagine and glutamine in biological fluids as trinitrophenyl derivatives. Nature (Lond.) 211, 602–604 (1966).Google Scholar
  40. Broome, J. D.: L-Asparaginase: the evolution of a new tumor inhibitory agent. Trans. N.Y. Acad. Sci. 30, 690–704 (1968a).PubMedGoogle Scholar
  41. Broome, J. D.: Factors which may influence the effectiveness of L-asparaginases as tumor inhibitors. Brit. J. Cancer 22, 595–602 (1968b).PubMedGoogle Scholar
  42. Broome, J. D.: Studies on the mechanism of tumor inhibition by L-asparaginase. J. exp. Med. 127, 1055–1072 (1968c).PubMedGoogle Scholar
  43. Broome, J.D., Schwabtz, J. H.: Differences in the production of L-asparagine in asparaginase- sensitive and resistant lymphoma cells. Biochim. biophys. Acta (Amst.) 138, 637–639 (1967).Google Scholar
  44. Brown, C. H., Ill, Canellos, G. P., Cabbone, P. P.: Effect of L-asparaginase on mouse bone marrow, assayed by in vitro culture. Blood 36, 385–389 (1970).Google Scholar
  45. Burgio, G. R., Astaldi, A., Jr., KRC, I., Micju, D., Astaldi, G.: With reference to blastogenesis inhibition by L-asparaginase. Recent Res. Cancer Res. 33, 288–295 (1970).Google Scholar
  46. Campbell, H. A., Mashburn, L. T.: L-Asparaginase EC-2 from Escherichia coli. Some substrate specificity characteristics. Biochemistry 8, 3768–3775 (1969).PubMedGoogle Scholar
  47. Campbell, H. A., Mashburn, L. T., Boyse, E. A., Old, L.J.: TWO L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity. Biochemistry 6, 721–730 (1967).PubMedGoogle Scholar
  48. Canellos, G. P., Haskell, C. M.: Studies of resistance to L-asparaginase in human leukemia. Recent Res. Cancer Res. 33, 188–193 (1970).Google Scholar
  49. Canellos, G. P., Haskell, C. M., Abseneau, J., Cabbone, P. P.: Hypoalbuminemic and hypocholesterolemic effect of L-asparaginase (NSC-109, 229) treatment in man — a preliminary report. Cancer Chemother. Rep. 53, 67–69 (1969).Google Scholar
  50. Capizzi, R. L., Bertino, J. R., Handschumacher, R. E.: L-Asparaginase. Ann. Rev. Med. 21, 433–444 (1970).PubMedGoogle Scholar
  51. Cedar, H., Schwartz, J. H.: Localization of the two L-asparaginases in anaerobically grown Escherichia coli. J. biol. Chem. 242, 3753–3755 (1967).PubMedGoogle Scholar
  52. Chakrabarty, A. K., Friedman, H.: L-Asparaginase-induced immunosuppression: effects on antibody-forming cells and serum titers. Science 107, 869–870 (1970).Google Scholar
  53. Chaney, P. L., Marbach, E. P.: Modified reagents for determination of urea and ammonia. Clin. Chem. 8, 130–132 (1962).PubMedGoogle Scholar
  54. Chang, T. M. S.: The in vivo effects of semipermeable microcapsules containing L-asparaginase on 6C3HED lymphosarcoma. Nature (Lond.) 229, 117–118 (1971).Google Scholar
  55. Chou, T. C., Handschumacher, R. E.: Kinetic mechanism of L-asparagine synthetase of 6C3HED—RG1 tumor. Fed. Proc. 29, 407 (1970).Google Scholar
  56. Clementi, A.: La désamidation enzymatique de l’asparagine chez les différentes espèce- animales et la signification physiologique de sa présence dans l’organisme. Arch. int. Physiol. 19, 369–398 (1922).Google Scholar
  57. Connors, T. A., Jones, M.: The effect of asparaginase on some animal tumors. Recent Res. Cancer Res. 83, 181–187 (1970).Google Scholar
  58. Cooney, D. A., Capizzi, R. L., Handschumacjher, R. E.: Evaluation of L-asparagine metabolism in animals and man. Cancer Res. 30, 929–935 (1970).PubMedGoogle Scholar
  59. Cooney, D. A., Davis, R. D.: The stability of L-asparaginase with respect to protein dénaturants. Biochim. biophys. Acta (Amst.) 212, 134–138 (1970).Google Scholar
  60. Cooney, D. A., Davis, R. D., Van Atta, G.: A spectrophotometric method for the simultaneous measurement of L-glutamine and L-asparagine in biological materials. Anal. Biochem. 40, 312–326 (1971).PubMedGoogle Scholar
  61. Cooney, D. A., Handscbumacher, R. E.: L-Asparaginase and L-asparagine metabolism. Ann. Rev. Pharmacol. 10, 421–440 (1970).PubMedGoogle Scholar
  62. Dartnall, J. A.: L-Asparaginase and blastogenesis. Lancet II, 1357–1358 (1969).Google Scholar
  63. De-Angeli, L. C., Pocchiari, F., Russi, S., Tonolo, A., Zurita, V. E., Ciaranfi, E., Perin, A.: Effect of L-asparaginase from Aspergillus terreus on ascites sarcoma in the rat. Nature (Lond.) 225, 549–550 (1970).Google Scholar
  64. De Barbieri, A., Astaldi, A., Jr., Micu, D., Mistretta, A. P., Astaldi, G., Burgio, G. R.: Relationship between L-asparaginase blood level and inhibition of lymphocyte blasto-genesis. Boll. 1st. sieroter. Milan. 49, 382–389 (1970).Google Scholar
  65. Debarros, T., Filho, M. C., Ferreira De Santana, C., Valenca, M., Pereira Da Silva, M., Guedes, J., De Carvalho, A. R. L.: Utilizacao de L’asparaginase em paciente humano portador de neoplasia malignana. An. Fac. Med. Recife 25, 21–28 (1965).Google Scholar
  66. De Groot, N., Lichtenstein, N.: The action of Pseudomonas fluorescens extracts on aspara- gine and asparagine derivatives. Biochim. biophys. Acta (Amst.) 40, 99–110 (1960).Google Scholar
  67. Deodhar, S. D.: Enhancement of metastases by L-asparaginase in a mouse tumour system. Nature (Lond.) 281, 319–321 (1971).Google Scholar
  68. Deutsch, E., Fischer, M., Frischauf, H., Honetz, N., Lechner, K., Pesendorfer, F., Stych, H., Weissmann, A.: Blood coagulation changes under L-asparaginase therapy. Recent Res. Cancer Res. 33, 331–341 (1970).Google Scholar
  69. Dolowy, W. C., Elrod, L. M., Ammeraal, R. N., Schrek, R.: Toxicity of L-asparaginase to resistant and susceptible lymphoma cells in vitro. Proc. Soc. exp. Biol. (N. Y.) 125, 598–601 (1967).Google Scholar
  70. Dolowy, W. C., Henson, D., Cornet, J., Sellin, H.: Toxic and antineoplastic effects of L- asparaginase. Cancer 19, 1813–1819 (1966).PubMedGoogle Scholar
  71. Dolowy, W. C., Schrek, R., Henson, D., Cornet, J., Brown, E.: Effects of guinea-pig serum on the Walker 256 carcinosarcoma. Nature (Lond.) 218, 1028–1031 (1968).Google Scholar
  72. Dox, A. W.: The intracellular enzymes of lower fungi, especially those of Pénicillium camemberti. J. biol. Chem. 6, 461–467 (1909).Google Scholar
  73. Eagle, H.: The specific amino acid requirements of a mammalian cell (strain L) in tissue culture. J. biol. Chem. 214, 839–852 (1955).PubMedGoogle Scholar
  74. Ehrman, M., Cedar, H., Schwartz, J. H.: L-Asparaginase II of Escherichia coli. Studies on the enzymatic mechanism of action. J. biol. Chem. 246, 88–94 (1971).PubMedGoogle Scholar
  75. Ellem, K. A. O., Fabrizio, A. M., Jackson, L.: The dependence of DNA and RNA synthesis on protein synthesis in asparaginase-treated lymphoma cells. Cancer Res. 30, 515–527 (1970).PubMedGoogle Scholar
  76. Eremenko, V. V., Evseev, L. P., Nikolaev, A. Y.: Asparaginaza Bacterium cadaveris. Mikro- biologiya 37, 207–212 (1968).Google Scholar
  77. Evseev, L. P., Nikolaev, A. Y.: Indutsirovannoe obrazovanie sintetaz asparagina i gliutamina u Pseudomonas sp. Biokhimiya 33, 1106–1110 (1968).Google Scholar
  78. Fidler, I. J.: L-Asparaginase and metastasis. Lancet I, 777–778 (1970).Google Scholar
  79. Fidler, I. J.: Duration of in vivo effects of L-asparaginase on experimental metastasis. Nature (Lond.) 229, 564 (1971).Google Scholar
  80. Fink, U., Begemann, H.: Clinical studies with L-asparaginase in dermatomyositis. Recent Res. Cancer Res. 33, 329–330 (1970).Google Scholar
  81. Frank, B. H., Pekar, A. H., Veros, A. J., HO, P. P. K.: Crystalline L-asparaginase from Escherichia coli B. II. Physical properties, subunits, and reconstitution behavior. J. biol. Chem. 245, 3716–3724 (1970).PubMedGoogle Scholar
  82. Friedman, H.: L-Asparaginase induced immunosuppression: inhibition of bone marrow derived antibody precursor cells. Science 174, 139–141 (1971).PubMedGoogle Scholar
  83. Frohwein, Y. Z., Friedman, M., Reizer, J., Grossowicz, N.: Sensitive and rapid assay for L-asparaginase. Nature New Biol. 230, 158–159 (1971).PubMedGoogle Scholar
  84. Galaev, Y. V., Kharats, K. S.: Izuchenie aktinvnosfi L-asparaginazy u kishechnol palochki razlichnykh tipov. Zh. Mikrobiol. (mosk.) 46, 127–131 (1969).Google Scholar
  85. Gallo, R. C., Longmore, J. L., Adamson, R. H.: Asparaginyl-tRNA and resistance of murine leukaemias to L-asparaginase. Nature (Lond.) 227, 1134–1136 (1970).Google Scholar
  86. Greenquist, A. C., Wriston, J. C., Jr.: On the structure of L-asparaginase from Escherichia coli B. Fed. Proc. 29, 882 (1970).Google Scholar
  87. Greenstein, J. P., Carter, C. E.: Influence of a-keto acids on the desamidation of amino acid amides. J. nat. Cancer Inst. 7, 57 — 60 (1946).PubMedGoogle Scholar
  88. Greenstein, J. P., Price, V. E.: a-Keto acid-activated glutaminase and asparaginase. J. biol. Chem. 178, 695 — 705 (1949).PubMedGoogle Scholar
  89. Grover, C. E., Chibnall, A. C.: The enzymic deamidation of asparagine in the higher plants. Biochem. J. 21, 857 — 868 (1927).PubMedGoogle Scholar
  90. Guarino, A. M., Söhroeder, D. H., Adamson, R. H., Call, J. B., Gram, T. E.: Studies of hepatic microsomal enzymes, serum proteins, and serum cholesterol after treatment of rats with L-asparaginase alone or in combination with phenobarbital. J. nat. Cancer Inst. 45, 783–787 (1970).PubMedGoogle Scholar
  91. Haley, E. E., Fischer, G. A., Welch, A. D.: The requirement for L-asparagine of mouse leu-kemia cells L5178Y in culture. Cancer Res. 21, 532–536 (1961).PubMedGoogle Scholar
  92. Hall, J. G.: The partitioning of L-asparaginase between blood and lymph. Ree. Res. Cancer Res. 38, 75–80 (1970).Google Scholar
  93. Halpern, Y. S., Grossowicz, N.: Hydrolysis of amides by extracts from mycobacteria. Bio-chem. J. 65, 716–720 (1957).Google Scholar
  94. Handschumacher, R. E.: Asparaginase: chemical structure and its relation to disposition and therapeutic efficacy. Colloq. Intern. Centre Nat. Rech. Seien. (Paris) 197, 377–386 (1971).Google Scholar
  95. Harris, J. E.: Effect of L-asparaginase on the ability of normal mouse bone marrow to form soft agar colonies. Nature (Lond.) 223, 850–851 (1969).Google Scholar
  96. Haskell, C. M., Canellos, G. P.: L-Asparaginase resistance in human leukemia-asparagine synthetase. Biochem. Pharmacol. 18, 2578–2580 (1969).PubMedGoogle Scholar
  97. Haskell, C. M., Canellos, G. P., Cooney, D. A., Hansen, H. H.: Biochemical and pharmacologic effects of L-asparaginase in man. J. Lab. clin. Med. 75, 763–770 (1970).PubMedGoogle Scholar
  98. Heene, D. L., Löffler, H.: The hemostatic defect induced by treatment with asparaginase in leukemia. Recent Res. Cancer Res. 33, 342–343 (1970).Google Scholar
  99. Heinemann, B., Howard, A. J.: Production of tumor-inhibitory L-asparaginase by submerged growth of Serratia marcescens. Appi. Microbiol. 18, 550–554 (1969).Google Scholar
  100. Hersh, E. M.: L-Glutaminase: suppression of lymphocyte blastogenic responses in vitro. Science 172, 736–738 (1971).PubMedGoogle Scholar
  101. Hersh, E. M., Brown, B. W.: Inhibition of immune responses by glutamine antogonism: effect of azotomycin on lymphocyte blastogenesis. Cancer Res. 31, 834–840 (1971).PubMedGoogle Scholar
  102. Hill, J. M., Loeb, E., Hill, N. O., Maclellan, A., Khan, A., Alexander, T. R., Adachi, M.: Treatment of acute leukemia with L-asparaginase. Progr. Antimicrob. Anticancer Chemother. 2, 667–678 (1970).Google Scholar
  103. Hill, J. M., Loeb, E., Maclellan, A., Khan, A., Roberts, J., Shields, W. F., Hill, N. O.: Response to highly purified L-asparaginase during therapy of acute leukemia. Cancer Res. 29, 1574–1580 (1969).PubMedGoogle Scholar
  104. Hill, J. M., Roberts, J., Loeb, E., Khan, A., Maclellan, A., Hill, R. W.: L-Asparaginase therapy for leukemia and other malignant neoplasms. J. Amer. med. Assoc. 202, 882–888 (1967).Google Scholar
  105. Ho, D. H. W., Whitecar, J. P., Jr., Luce, J. K., Frei, E., III: L-Asparagine requirement and the effect of L-asparaginase on the normal and leukemic human bone marrow. Cancer Res. 30, 466–472 (1970).PubMedGoogle Scholar
  106. Ho, P. P. K., Frank, B. H., Burck, P. J.: Crystalline L-asparaginase from Escherichia coli B. Science 165, 510–512 (1969).PubMedGoogle Scholar
  107. Ho, P. P. K., Milikin, E. B., Bobbitt, J. L., Grinnan, E. L., Burck, P. J., Frank, B. H., Boeck, L. D., Squires, R. W.: Crystalline L-asparaginase from Escherichia coli B. I. Purification and chemical characterization. J. biol. Chem. 245, 3708–3715 (1970).PubMedGoogle Scholar
  108. Hobik, H. P.: Immunosuppressive Wirkung von L-asparaginase in der Graft-Versus-Host Reaktion. Naturwissenschaften 56, 217 (1969).PubMedGoogle Scholar
  109. Holcenberg, J. S.: Guinea pig asparagine synthetase. Biochim. biophys. Acta (Amst.) 185, 228–238 (1969).Google Scholar
  110. Holcenberg, J. S., Pease, J.: Asparagine synthesis in guinea-pig liver. Biochim. biophys. Acta (Amst.) 158, 500–502 (1968).Google Scholar
  111. Holmquist, N. D.: Effect of normal agouti serum on 6C3HED lymphoma in vivo. Fed. Proc. 21, 166 (1962).Google Scholar
  112. Horowitz, B., Madras, B. K., Meister, A., Old, L. J., Boyse, E. A., Stockert,E.: Asparagine synthetase activity of mouse leukemias. Science 160, 533–535 (1968).PubMedGoogle Scholar
  113. Horowitz, B., Meister, A.: Asparagine synthetase from RADA1 leukemia cells. Colloq. Intern. Centre nat. Rech. Scien. (Paris) 197, 87–91 (1971).Google Scholar
  114. Horowitz, B., Nelson, J. A., Meister, A.: Asparagine synthetase (tumor cells). Meth. Enzymol. 17, 726–732 (1970).Google Scholar
  115. Irion, E., Arens, A.: Biochemical characterization of L-asparaginases from E. coli. Recent Res. Cancer Res. 83, 39–47 (1970).Google Scholar
  116. Jackson, R. C., Handschumacher, R. E.: Escherichia coli L-asparaginase. Catalytic activity and subunit nature. Biochemistry 9, 3585–3590 (1970).Google Scholar
  117. Jahnes, W. G., LI, C. P., Tauraso, N. M.: Studies on inhibition of viral oncogenesis. II. Inhibitory effect of L-asparaginase, clam liver extract and methotrexate on Rous virus focus formation. Arch. ges. Virusforsch. 82, 236–243 (1970).Google Scholar
  118. Jameson, E., Ainis, H., Ryan, R. M.: Action of guinea pig serum and human gamma globulin on growth of a rat tumor. Science 124, 980–981 (1956).PubMedGoogle Scholar
  119. Jameson, E., Ainis, H., Ryan, R. M.: The inhibition by guinea pig serum of the growth of the Murphy-Sturm lymphosarcoma. Cancer Res. 18, 866–868 (1958).PubMedGoogle Scholar
  120. Jayaram, H. N., Ramakrishnan, T., Vaidyanathan, C. S.: L-Asparaginases from Mycobacterium tuberculosis strains H37RW and H37R0. Arch. Biochem. Biophys. 126, 165–174 (1968).PubMedGoogle Scholar
  121. Kessel, D.: Asparaginyl-transfer RNA: a substrate for L-asparaginase. Biochim. biophys. Acta (Amst.) 240, 554–557 (1971).Google Scholar
  122. Kessel, D., Bosmann, H. B.: Effects of L-asparaginase on protein and glycoprotein synthesis. FEBS Let. 10, 85–88 (1970).Google Scholar
  123. Khan, A., Hill, J. M.: Suppression of skin hypersensitivity and antibody formation by L- asparaginase. J. Immunol. 104, 679–684 (1970).PubMedGoogle Scholar
  124. Khan, A., Hill, J. M., Adachi, M.: L-Asparaginase in experimental auto-immune disease: inhibition of allergic encephalomyelitis. J. Immunol. 105, 256–258 (1970).Google Scholar
  125. Kidd, J. G.: Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum. J. exp. Med. 98, 565–582 (1953 a).Google Scholar
  126. Kidd, J. G.: Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. II. Studies on the nature of the active serum constituent: histological mechanism of the regression: tests for effects of guinea pig serum on lymphoma cells in vitro: discussion. J. exp. Med. 98, 583–606 (1953b).PubMedGoogle Scholar
  127. Kidd, J. G.: Effects of arsenic-azoproteins on mouse lymphoma cells in vivo with observations on the effects of other “anti-lymphoma” agents, and on the susceptibility to these effects of lymphoma cells of various types. J. exp. Med. 108, 665–684 (1958).PubMedGoogle Scholar
  128. Kidd, J. G.: Asparaginase and cancer — yesterday and today. Rec. Res. Cancer Res. 38, 3–14 (1970).Google Scholar
  129. Kirschbaum, J., Wriston, J. C., Jr., Ratych, O. T.: Subunit structure of L-asparaginase from Escherichia coli B. Biochim. biophys. Acta (Amst.) 194, 161–169 (1969).Google Scholar
  130. Kojima, Y., Wacker, W. E. C.: An enzymatic method for the measurement of asparagine and a new assay of asparaginase activity. J. Lab. clin. Med. 74, 521–526 (1969).PubMedGoogle Scholar
  131. Kretovich, W. L.: The biosynthesis of dicarboxylic amino acids and enzymic transformations of amides in plants. Advanc. Enzymol. 20, 319–340 (1958).Google Scholar
  132. Kristiansen, T., Einarsson, M., Sundberg, L., Porath, J.: Purification of L-asparaginase from E. coli by specific adsorption and desorption. FEBS Let. 7, 294–296 (1970).Google Scholar
  133. Krzeminski, Z.: Dalsze badania nad dezaminacja aminokwasow drzez Streptococcus mitis. 2. Dezeminacja asparaginy. Cz. Stomat. 22, 249–254 (1969).Google Scholar
  134. Kwak, K. S., Jameson, E., Ryan, R. M., Kurtz, H. M.: The effect of varying implant cell numbers on the inhibitory activity of guinea pig serum on Walker carcinosarcoma 256 in the rat. Cancer Res. 21, 44–47 (1961).PubMedGoogle Scholar
  135. Laboureur, P.: Biochimie de L’asparaginase. Propriétés du système asparaginase et activité biologique. Pathol. Biol. 17, 885–908 (1969).PubMedGoogle Scholar
  136. Laboureur, P., Langlois, C., Labrousse, M., Boudon, M., Emeraud, J., Samain, J. F.: Différentes formes d’asparaginases de E. coli. Colloq. int. Centre nat. Rech. Scien. (Paris) 197, 43–53 (1971).Google Scholar
  137. Lajolo, D., Astaldi, A., Jr., Pecco, P., Bert, G., Astaldi, G.: Electrophoretical mobility of human lymphocytes in the presence of E. coli L-asparaginase. Exp. cell Res. 60, 458–459 (1970).PubMedGoogle Scholar
  138. Lang, S.: Über Desamidierung im Tierkörper. Beitr. ehem. Physiol. Path. 5, 321–345 (1904).Google Scholar
  139. Lauenstein, K., Grundmann, E., Hobik, H. P., Madaus, W. P.: Experimental immunosuppression with L-asparaginase. Recent Res. Cancer Res. 33, 170–173 (1970).Google Scholar
  140. Lauinger, C., Ressler, C.: β-Cyanoalanine as a substrate for asparaginase. Stoichiometry, kinetics, and inhibition. Biochim. biophys. Acta (Amst.) 198, 316–323 (1970).Google Scholar
  141. Lees, E. M., Blakeney, A. B.: The distribution of asparaginase activity in legumes. Biochim. biophys. Acta (Amst.) 215, 145–151 (1970).Google Scholar
  142. Levintow, L.: Evidence that glutamine is a precursor of asparagine in a human cell in tissue culture. Science 126, 611–612 (1957).PubMedGoogle Scholar
  143. Litt, Y. P., Handschumacher, R. E.: Chemical modification of L-asparaginase. Proc. Amer. Ass. Cancer Res. 12, 99 (1971).Google Scholar
  144. Lorke, D., Tettenborn, D.: Experimental studies on the toxicity of crasnitin in animals. Recent Res. Cancer Res. 33, 174–180 (1970).Google Scholar
  145. Maral, R., Guyonnet, J. C., Julou, L., Deratuld, Y., Werner, G. H.: Studies on the immunosuppressive activity of L-asparaginase. Ree. Res. Cancer Res. 33, 160–169 (1970).Google Scholar
  146. Maral, R., Werner, G. H.: Antiviral activity of L-asparaginase. Nature New Biol. 232, 187–188 (1971).PubMedGoogle Scholar
  147. Mardashev, S. R., Shao, H. W.: Purification of guinea pig serum asparaginase by chromatography on a diethylaminoethyl cellulose column. Dokl. Akad. Nauk. S.S.S.R. 142, 21–24 (1967).Google Scholar
  148. Marquardt, H.: L-Asparaginase — das erste spezifische Cytostaticum. Arzneimittel-Forsch. 18, 1380–1386 (1968).Google Scholar
  149. Mashburn, L. T., Gordon, C. S.: The effects of L-asparaginase on the amino acid incorporation of mouse lymphoid tumors. Cancer Res. 28, 961–967 (1968).PubMedGoogle Scholar
  150. Mashburn, L. T., Landin, L. M.: Changes in ribonuclease activities in P1798 lymphosarcoma after asparaginase treatment. Arch. Biochem. Biophys. 125, 721–726 (1968).PubMedGoogle Scholar
  151. Mashburn, L. T., Landin, L. M.: Some physicochemical aspects of L-asparaginase therapy. Recent Res. Cancer Res. 33, 48–57 (1970).Google Scholar
  152. Mashburn, L. T., Wriston, J. C., Jr.: Tumor inhibitory effect of L-asparaginase. Biochem. biophys. Res. Commun. 12, 50–55 (1963).Google Scholar
  153. Mashburn, L. T., Wriston, J. C., Jr.: Tumor inhibitory effect of L-asparaginase from Escherichia coli. Arch. Biochem. Biophys. 105, 450–452 (1964).PubMedGoogle Scholar
  154. Mashburn, L. T., Wriston, J. C., Jr.: Change in ribonuclease concentrations in L-asparaginase- treated lymphosarcomata. Nature (Lond.) 211, 1403–1404 (1966).Google Scholar
  155. McCoy, T. A., Maxwell, M., Irvine, E., Sartorelli, A. C.: TWO nutritional variants of cultured Jensen sarcoma cells. Proc. Soc. exp. Biol. (N. Y.) 100, 862 — 865 (1959b).Google Scholar
  156. McCoy, T. A., Maxwell, M., Kruse, P. F., Jr.: The amino acid requirements of the Jensen sarcoma in vitro. Cancer Res. 19, 591–595 (1959a).PubMedGoogle Scholar
  157. McElwain, T. J., Hayward, S. K.: L-Asparaginase and blastogenesis. Lancet I, 527 (1969).Google Scholar
  158. Meister, A.: Glutaminase, asparaginase, and a-keto acid-co-amidase. B. L-Asparaginase from guinea pig serum. Meth. Enzymol. 2, 383–385 (1955).Google Scholar
  159. Meister, A.: Intermediary metabolism of the amino acids. In: Meister, A. (Ed.): Biochemistry of the Amino Acids, Vol. II, 2 nd. Edition,pp. 606–617. New York: Academic Press 1965.Google Scholar
  160. Meister, A., Sober, H. A., Tice, S. V., Fraser, P. E.: Transamination and associated deamidation of asparagine and glutamine. J. biol. Chem. 197, 319–330 (1952).PubMedGoogle Scholar
  161. Micou, D., Astaldi, G., Astaldi, A., Jr., Mihailesco, E., Lisiewicz, J.: L’effet de la L-as- paraginase sur les cellules de la série plasmocytaire. Schweiz, med. Wschr. 100, 1997–1999 (1970).Google Scholar
  162. Mikucki, J., Szabapinska-Kwaszewska, J., Krzeminski, Z.: Aktywnoéé asparaginazy u anty- biotykoopornych gronkowcow ziocistych. Med. Doswiadczalna Mikrobiol. 20, 227–231 (1968).Google Scholar
  163. Miller, D. S., Marlborough, D. I., Cammaök, K. A.: Physical properties and subunit structure of L-asparaginase isolated from Erwinia carotovora. Colloq. int. Centre nat. Rech. Seien. (Paris) 197, 55–71 (1971).Google Scholar
  164. Miller, H. K., Balis, M. E.: Glutaminase activity of L-asparagine amidohydrolase. Biochem. Pharmacol. 18, 2225–2232 (1969).PubMedGoogle Scholar
  165. Miller, H. K., Krakoff, I. H., Salser, J. S., Balis, M. E.: Sensitivity to L-asparaginase and amino acid metabolism. J. nat. Cancer Inst. 44, 1129–1139 (1970).PubMedGoogle Scholar
  166. Miller, H. K., Salser, J. S., Balis, M. E.: Amino acid levels following L-asparagine amidohydrolase (EC. 3.5.1.1) therapy. Cancer Res. 29, 183–187 (1969).PubMedGoogle Scholar
  167. Miller, J. F. A. P., Mitchell, G. F.: Thymus and antigen reactive cells. Transplant. Rev. 1, 3–42 (1969).PubMedGoogle Scholar
  168. Mittra, M., Hirano, M., Kakizawa, K., Morita, A., Uetani, T., Yamada, K.: Inhibitory effect of L-asparaginase in lymphocyte transformation induced by phytohemagglutinin. Cancer Res. 30, 768–772 (1970a).Google Scholar
  169. Miura, M., Hirano, M., Kakizawa, K., Morita, A., Uetani, T., Yamada, K.: Antitumor activity of L-β-aspartohydroxamic acid in vivo. Screening data of 21 L-asparagine related compounds. Progr. antimicrob. anticancer Chemotherapy 2, 170 — 174 (1970b).Google Scholar
  170. Miura, M., Kawashima, K., Uetani, T., Hirano, M., Kakizawa, H., Ohno, R., Morita, A., Nishiwaki, H., Yamada, K.: Influence of L-asparaginase on antibody production and growth of tumors in allogeneic mice. Cancer Res. 31, 114–121 (1971).PubMedGoogle Scholar
  171. Morrow, J.: Mutation rate from asparagine requirement to asparagine non-requirement. J. cell. Physiol. 77, 423–425 (1971).PubMedGoogle Scholar
  172. Nahorski, S. R.: Fluorometric measurement of glutamine and asparagine using enzyme methods. Anal. Biochem. 42, 136–142 (1971).PubMedGoogle Scholar
  173. Nakamura, N., Morikawa, Y., Tanaka, M.: L-Asparaginase from Escherichia coli. II. Sub-strate specificity studies. Agr. biol. Chem. 35, 743–751 (1971).Google Scholar
  174. Nelson, S. D., Lee, M. B., Bridges, J. M.: Immunosuppressive activity of L-asparaginase in mice. Transplantation 9, 566–570 (1970).PubMedGoogle Scholar
  175. Neuman, R. E., McCoy, T. A., The dual requirement of the Walker carcinosarcoma 256 in vitro for asparagine and glutamine. Science 124, 124–125 (1956).PubMedGoogle Scholar
  176. Nicolin, A., Napoli, P. A.: Azione favorente delia levo-asparaginasi sulla crescita del car-cinoma ascite di Ehrlich (in animali normali o in animali previamente “vaccinati” verso lo stesso tumore ascitico). Arch. ital. Pat. 12, 177–187 (1969).Google Scholar
  177. Nishimura, Y., Makino, H., Takenaka, O., Inada,Y.: Amino acid residues in asparaginase (Escherichia coli HAP) associated with its enzymic activity. Biochim. biophys. Acta (Amst.) 227, 171–179 (1971).Google Scholar
  178. North, A. C. T., Wade, H. E., Cammack, K. A.: Physiochemical studies of L-asparaginase from Erwinia carotovora. Nature (Lond.) 224, 594–595 (1967).Google Scholar
  179. Oettgen, H. F., Old, L. J., Boyse, E. A., Campbell, H. A., Philips, F. S., Clarkson, B. D., Tallal, L., Leeper, R. D., Schwartz, M. K., Kim, J. H.: Inhibition of leukemias in man by L-asparaginase. Cancer Res. 27, 2619–2631 (1967).PubMedGoogle Scholar
  180. Ohno, R., Harris, J. E., Hersh, E. M.: L-Asparaginase: suppression of the immune response of mice to sheep red blood cells. Clin. exp. Immunol. 7, 221–227 (1970).PubMedGoogle Scholar
  181. Ohno, R., Hersh, E. M.: Immunosuppressive effects of L-asparaginase. Cancer Res. 30, 1605–1611 (1970a).PubMedGoogle Scholar
  182. Ohno, R., Hersh, E. M.: The inhibition of lymphocyte blastogenesis by L-asparaginase (LA). Blood 35, 250–262 (1970b).PubMedGoogle Scholar
  183. Ohnuma, T., Bergel, F., Bray, R. C.: Enzymes in cancer. Asparaginase from chicken liver. Biochem. J. 103, 238–245 (1967).PubMedGoogle Scholar
  184. Ohnuma, T., Holland, J. F., Freeman, A., Sinks, L. F.: Biochemical and pharmacological studies with asparaginase in man. Cancer Res. 30, 2297–2305 (1970).PubMedGoogle Scholar
  185. Old, L. J., Boyse, E. A., Campbell, H. A.: L-Asparagine and leukemia. Sci. Amer. 219, 34–40 (1968).PubMedGoogle Scholar
  186. Old, L. J., Boyse, E. A., Campbell, H. A., Daria, G. M.: Leukaemia-inhibiting properties and L-asparaginase activity of sera from certain South American rodents. Nature (Lond.) 198, 801 (1963).Google Scholar
  187. Osoba, D.: Restriction of the capacity to respond to two antigens by single precursors of antibody-producing cells in culture. J. exp. Med. 129, 141–152 (1969).PubMedGoogle Scholar
  188. Patterson, M.K., Jr.: Studies on the control of asparagine biosynthesis in mammalian tissues. Rec. Res. Cancer Res. 33, 22–30 (1970).Google Scholar
  189. Patterson, M.K., Jr.: Effects of L-asparaginase on asparagine synthetase levels of normal and malignant tissues. Colloq. int. Centre nat. Rech. Scien. (Paris) 197, 107–113 (1971).Google Scholar
  190. Patterson, M. K., Jr., Conway, E., Whittle, W., McCoy, T. A.: In vitro effects of guinea pig serum on the Jensen, JA-1 and JA-2 sarcomas. Proc. Soc. exp. Biol. (N.Y.) 119, 5–9 (1965).Google Scholar
  191. Patterson, M. K., Jr., Maxwell, M. D.: Effects of L-asparagine deprivation on the cell cycle of the Jensen sarcoma. Cancer Res. 30, 1064–1067 (1970).PubMedGoogle Scholar
  192. Patterson, M. K., Jr., Maxwell, M. D., Conway, E.: Studies on the asparagine requirement of the Jensen sarcoma and the derivation of its nutritional variant. Cancer Res. 29, 296–300 (1969).PubMedGoogle Scholar
  193. Patterson, M. K., Jr., Orr, G.: L-Asparagine biosynthesis by nutritional variants of the Jensen sarcoma. Biochem. biophys. Res. Commun. 26, 228–233 (1967).Google Scholar
  194. Patterson, M. K., Jr., Orr, G. R.: Asparagine biosynthesis by the Novikoff hepatoma. Isola-tion, purification, property, and mechanism studies of the enzyme system. J. biol. Chem. 243, 376–380 (1968).PubMedGoogle Scholar
  195. Patterson, M. K., Jr., Orr, G. R.: Regeneration, tumor, dietary, and L-asparaginase effects on asparagine biosynthesis in rat liver. Cancer Res. 29, 1179–1183 (1969).PubMedGoogle Scholar
  196. Patterson, M. K., Jr., Orr, G. R., McCoy, T. A.: Asparagine-C14 and glutamine-C14 from animal cell protein and their chemical degradation. Anal. Biochem. 6, 543–548 (1963).PubMedGoogle Scholar
  197. Peters, J. H., Lin, S. C., Berridge, B. J., Jr., Ceao, W. R., Cummings, J. G.: Circulatory L- asparaginase activity in primates. Life Sci. 9, 431–436 (1970).Google Scholar
  198. Peterson, R. E., Ciegler, A.: L-Asparaginase production by various bacteria. Appl. Microbiol. 17, 929–930 (1969a).PubMedGoogle Scholar
  199. Peterson, R. E., Ciegler, A.: L-Asparaginase production by Erwinia aroideae. Appl. Microbiol. 18, 64–67 (1969b).PubMedGoogle Scholar
  200. Peterson, R.G., Handschumacher, R. E., Mitchell, M. S.: Immunological responses to L- asparaginase. J. clin. Invest. 50, 1080–1090 (1971).PubMedGoogle Scholar
  201. Prager, M. D., Bachynsky, N.: Asparagine synthetase in asparaginase resistant and susceptible mouse lymphomas. Biochem. biophys. Res. Commun. 31, 43–47 (1968a).Google Scholar
  202. Prager, M. D., Bachynsky, N.: Asparagine synthetase in normal and malignant tissues; correlation with tumor sensitivity to asparaginase. Arch. Biochem. Biophys. 127, 645–654 (1968b).PubMedGoogle Scholar
  203. Prager, M. D., Derr, I.: Inhibition of primary antibody response by E. coli asparaginase. Nature (Lond.) 225, 952 (1970).Google Scholar
  204. Prager, M. D., Derr, I.: Metabolism of asparagine, aspartate, glutamine, and glutamate in lymphoid tissue: basis for immunosuppression by L-asparaginase. J. Immunol. 106, 975–979 (1971).PubMedGoogle Scholar
  205. Prusiner, S., Milner, L.: A rapid radioactive assay for glutamine synthetase, glutaminase, asparagine synthetase and asparaginase. Anal. Biochem. 37, 429–438 (1970).PubMedGoogle Scholar
  206. Putter, J.: Pharmacokinetic behavior of L-asparaginase in men and in animals. Recent Res. Cancer Res. 33, 64–74 (1970).Google Scholar
  207. Rauenbusch, E., Batjer, K., Kaufmann, W., Wagner, O.: Isolation and crystallization of L-asparaginase from E. coli. Recent Res. Cancer Res. 33, 31–38 (1970).Google Scholar
  208. Rauenbusch, E., Irion, E., Arens, A.: The subunits of L-asparaginase from Escherichia coli. Colloq. int. Centre nat. Rech. Scien. (Paris) 197, 31–42 (1971).Google Scholar
  209. Ravel, J. M., Norton, S. J., Humphreys, J. S., Shive, W.: Asparagine biosynthesis in Lactobacillus arabinosus and its control by asparagine through enzyme inhibition and repression. J. biol. Chem. 237, 2845–2849 (1962).PubMedGoogle Scholar
  210. Reddy, V. V. S., Jayaram, H. N., Sirsi, M., Ramakrishnan, T.: Inhibitory activity of L-as-paraginase from Mycobacterium tuberculosis on Yoshida ascites sarcoma in rats. Arch. Biochem. Biophys. 132, 262–267 (1969).PubMedGoogle Scholar
  211. Riley, V.: Influence of a benign virus upon mouse leukemia during asparaginase therapy. Path, et Biol. 18, 757–764 (1970).Google Scholar
  212. Riley, V., Spaceman, D. H., Fitzmaurice, M. A.: Critical influence of an enzyme-elevating virus upon long-term remissions of mouse leukemia following asparaginase therapy. Recent Res. Cancer Res. 33, 81–101 (1970).Google Scholar
  213. Roberts, J., Burson, G., Hill, J. M.: New procedures for purification of L-asparaginase with high yield from Escherichia coli. J. Bact. 95, 2117–2123 (1968).PubMedGoogle Scholar
  214. Roberts, J., Prager, M. D., Bachynsky, N.: The antitumor activity of Escherichia coli L-as- paraginase. Cancer Res. 26, 2213–2217 (1966).PubMedGoogle Scholar
  215. Robison, R. S., Berk, B.: L-Asparaginase synthesis by Escherichia coli B. Biotechnol. Bioeng. 11, 1211–1225 (1969).PubMedGoogle Scholar
  216. Rowley, B., Wriston, J. C., Jr.: Partial purification and antilymphoma activity of Serratia marcescens L-asparaginase. Biochem. biophys. Res. Commun. 28, 160–165 (1967).PubMedGoogle Scholar
  217. Rudman, D., Vogler, W. R., Howard, C. H., Gerron, G. G.: Observations on the plasma amino acids of patients with acute leukemia. Cancer Res. 31, 1159–1165 (1971).PubMedGoogle Scholar
  218. Ryan, W. L., Dworak, J. E.: Amino acids of the 6C3HED lymphosarcoma following treatment with asparaginase. Cancer Res. 30, 1206–1209 (1970).PubMedGoogle Scholar
  219. Ryan, W. L., Sornson, H. C.: Glycine inhibition of asparaginase. Science 167, 1512–1513 (1970).PubMedGoogle Scholar
  220. St. Pierre, R. L., Tennenbaum, J. I., Folk, R. M.: L-Asparaginase and allograft immunity. Lancet II, 1365–1366 (1970).Google Scholar
  221. Scheetz, R. W., Whelan, H. A., Wriston, J. C., Jr.: Purification and properties of an L-as- paraginase from Fusarium tricinctum. Arch. Biochem. Biophys. 142, 184–189 (1971).PubMedGoogle Scholar
  222. Schein, P. S., Rakieten, N., Gordon, B. M., Davis,R. D., Rall, D. P.: The toxicity of Esche-richia coli L-asparaginase. Cancer Res. 29, 426–434 (1969).Google Scholar
  223. Schrek, R., Dolowy, W. C., Ammeraal, R. N.: L-Asparaginase: toxicity to normal and leu-kemic human lymphocytes. Science 155, 329–330 (1967).PubMedGoogle Scholar
  224. Schulten, H. K., Giraldo, G.: Influence of L-asparaginase preparations of E. coli and Agouti serum on the homograft reactivity in the mouse. Recent Res. Cancer Res. 33, 155–159 (1970).Google Scholar
  225. Schulten, H. K., Gibaldo, G., Boyse, E. A., Oettgen, H. F.: Immunosuppressive action of L-asparaginase. Lancet II, 644–645 (1969).Google Scholar
  226. Schwartz, J. H., Reeves, J. Y., Broome, J. D.: Two L-asparaginases from E. coli and their action against tumors. Proc. nat. Acad. Sei. (Wash.) 56, 1516–1519 (1966).Google Scholar
  227. Schwartz, M. K.: The distribution and clearance of L-asparaginase. Recent Res. Cancer Res. 33, 58–63 (1970).Google Scholar
  228. Schwartz, M. K., Lash, E. D., Oettgen, H. F., Tomao, F. A.: L-Asparaginase activity in plasma and other biological fluids. Cancer 25, 244–252 (1970).PubMedGoogle Scholar
  229. Schwartz, R. S.: Immunosuppression by L-asparaginase. Nature (Lond.) 224, 275–276 (1969).Google Scholar
  230. Seeber, S., Warneoke, P., Straub, O. C.: Zum Einfluß von E. coZi-L-asparaginase auf den Nucleinsäurestoffwechsel lymphatischer Rinderleukämiezellen. Arzneimittel-Forsch. 19, 1745–1748 (1969).Google Scholar
  231. Seeber, S., Weser, U.: Inhibition of 3H-thymidine incorporation into rat liver nuclei by E. coli L-asparaginase. Nature (Lond.) 225, 652–653 (1970).Google Scholar
  232. Serba, J. A.: Regulatory genetic changes in the origin of asparaginase-sensitive leukemias. Tenth International Cancer Congress, Abstr. 359–360 (1970).Google Scholar
  233. Shaw, M. T., Barnes, C.C., Madden, F. J. F., Bagshawe, K. D.: L-Asparaginase and pancreatitis. Lancet II, 721 (1970).Google Scholar
  234. Shons, A., Jetzer, T., Najarian, J. S.: Prolongation of skin homograft survival by L-asparagin- ase. Transplantation 10, 280–281 (1970).PubMedGoogle Scholar
  235. Simberkoff, M. S., Thomas, L.: Reversal by L-glutamine of the inhibition of lymphocyte mitosis caused by E. coli asparaginase. Proc. Soc. exp. Biol. (N. Y.) 133, 642–644 (1970).Google Scholar
  236. Simberkoff, M. S., Thorbecke, G. J., Thomas, L.: Studies of PPLO infection. V. Inhibition of lymphocyte mitosis and antibody formation by mycoplasmal extracts. J. exp. Med. 129, 1163–1181 (1969).PubMedGoogle Scholar
  237. Sinclair, N. R. ST. C., Elliott, E. V.: Neonatal thymectomy and hemolysin responses in in-bred mice. J. Immunol. 101, 251–255 (1968).Google Scholar
  238. Sobin, L. H., Kidd, J. G.: A metabolic difference between two lines of lymphoma 6C3HED cells in relation to asparagine. Proc. Soc. exp. Biol. (N.Y.) 119, 325–327 (1965).Google Scholar
  239. Sobin, L. H., Kidd, J. G.: Alterations in protein and nucleic acid metabolism of lymphoma 6C3HED—OG cells in mice given guinea pig serum. J. exp. Med. 123, 55–74 (1966).PubMedGoogle Scholar
  240. Staerk, J., Zwisler, O., Ronneberger, H.: A comparison of L-asparaginase from Erwinia aroideae and from Escherichia coli: biochemical and biological properties. Experientia (Basel) 27, 250–252 (1971).Google Scholar
  241. Steensholt, G.: On the distribution of asparaginase. Acta physiol. scand. 8, 342–347 (1944).Google Scholar
  242. Suld, H. M., Herbut, P. A.: Guinea pig serum and liver asparaginases. Purification and anti-tumor activity. J. biol. Chem. 240, 2234–2241 (1965).PubMedGoogle Scholar
  243. Suld, H. M., Herbut, P. A.: Guinea pig serum and liver L-asparaginases. Comparison of serum and papain-digested liver L-asparaginases. J. biol. Chem. 245, 2797–2801 (1970a).PubMedGoogle Scholar
  244. Suld, H. M., Herbut, P. A.: Immunological studies on guinea pig serum and liver L-asparaginases. Purification of L-asparaginases by antibody precipitation. J. biol. Chem. 245, 2802–2808 (1970b).PubMedGoogle Scholar
  245. Tanaka, M., Kagawa, T., Tatano, T., Mochizuki, K., Nakamura, N., Kohagura, M., Hill, J. M.: Antineoplastic crystalline L-asparaginase from E. coli. Progr. antimicrob. anticancer Chemother. 2, 260–266 (1970).Google Scholar
  246. Tower, D. B., Peters, E. L., Curtis, W. C.: Guinea pig serum L-asparaginase. Properties, purification, and application to determination of asparagine in biological samples. J. biol. Chem. 238, 983–993 (1963).PubMedGoogle Scholar
  247. Tsuji, Y.: Amidase action of bacteria. Naika Hokan. 4, 222–223 (1957).Google Scholar
  248. Ubuka, T., Meister, A.: Studies on the utilization of asparagine by mouse leukemia cells. J. nat. Cancer Inst. 46, 291–298 (1971).PubMedGoogle Scholar
  249. Vadlamudi, S., Padarathsingh, M., Bonmassar, E., Waravdekar, V., Goldin, A.: Studies on neutralization of L-asparaginase activity in vitro and in vivo. Cancer 27, 1321–1327 (1971).PubMedGoogle Scholar
  250. Vadlamudi, S., Padarathsingh, M., Waravdekar, V. S., Goldin, A.: Factors influencing the therapeutic activity of L-asparaginase (NSC 109229) in leukemic (L5178Y) mice. Cancer Res. 30, 1467–1472 (1970).PubMedGoogle Scholar
  251. Von Furth, O., Friedmann, M.: Über die Verbreitung asparaginspaltender Organfermente. Biochem. Z. 26, 435–440 (1910).Google Scholar
  252. Wade, H. E., Elsworth, R., Herbert, D., Keppie, J., Sargeant, K.: A new L-asparaginase with antitumour activity. Lancet II, 776–777 (1968).Google Scholar
  253. Wagner, O., Bauer, K., Irion, E., Rauenbusöh, E., Kaufmann, W., Arens, A.: Polyäthylenglykol zur Anreicherung und Kristallisation von L-Asparaginase. Angew. Chem. 81, 904–905 (1969a).Google Scholar
  254. Wagner, O., Irion, E., Bauer, K.: Partially deaminated L-asparaginase. Biochem. biophys, Res. Commun. 37, 383–392 (1969b).Google Scholar
  255. Weinberger, S.: L-Asparaginase as an antitumor agent. Enzyme 12, 143–159 (1971).Google Scholar
  256. Weiner, M. S., Waithe, W. I., Hirschhorn, K.: L-Asparaginase and blastogenesis. Lancet II, 748 (1969).Google Scholar
  257. Weksler, M. E., Weksler, B. B.: Studies on the immunosuppressive properties of asparagin-ase. Immunology 21, 137–150 (1971).PubMedGoogle Scholar
  258. Whelan, H. A., Wriston, J. C., Jr.: Purification and properties of asparaginase from Escherichia coli B. Biochemistry 8, 2386–2393 (1969).PubMedGoogle Scholar
  259. Whitecar, J. P.,Jr.,Bodey, G. P., Hill, C. S., Jr., Samaan, N. A.: Effect of L-asparaginase on carbohydrate metabolism. Metabolism 19, 581–586 (1970).Google Scholar
  260. Woods, J. S., Lee, I. P., Dixon, R. L.: Asparagine incorporation into the DNA of hepatic and 6C3HED murine lymphosarcoma cells. Cancer Res. 30, 1210–1211 (1970).PubMedGoogle Scholar
  261. Wriston, J. C., Jr.: Asparaginase. Meth. Enzymol. 17, 732 — 742 (1970).Google Scholar
  262. Wriston, J. C., Jr.: L-Asparaginase. Enzymes 4, 101 — 121 (1971a).Google Scholar
  263. Wriston, J. C., Jr.: On the structure of E. coli B asparaginase. Colloq. int. Centre nat. Rech. Seien. (Paris) 197, 25–29 (1971b).Google Scholar
  264. Yellin, T. O., Wriston, J.C., Jr.: Purification and properties of guinea pig serum asparaginase. Biochemistry 5, 1605–1612 (1966).PubMedGoogle Scholar

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© springer-Verlag Berlin-Heidelberg 1975

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