Advertisement

Lactic Dehydrogenase Virus

  • K. E. K. Rowson
  • B. W. J. Mahy
Part of the Virology Monographs / Die Virusforschung in Einzeldarstellungen book series (VIROLOGY, volume 13)

Abstract

Inapparent virus infections of experimental animals and tissue culture systems present to the investigator a problem which it is impossible to overcome completely. Although all recognised viruses can be excluded from an experimental system, previously unsuspected viruses causing no obvious effects (‘silent’ viruses) will continue to be discovered. A truly silent virus would replicate, causing no change in its host cell, damage to infected tissue or immune response and would presumably be of no consequence. It is the relatively silent viruses which cause virtually no pathological changes but can alter the response of a test system, which are important. The lactic dehydrogenase virus (LDV) is an interesting example of such a virus. It causes no clinical disease in mice but can significantly alter their response to other infective agents and to the development of tumours. If the ideal virus is one which replicates rapidly and continuously without killing its host and is easily transmitted, LDV must be almost perfect. It replicates very rapidly in mice of all strains so far tested, produces a stable infection with a continuously high level of infective virus in the blood for the remainder of the animal’s life, yet causes no harm to its host. It lacks, however, one important property; the ability to pass readily from one animal to another under natural conditions. Infected females often fail to infect their young and transmission between adults is not very frequent. However, no doubt because of the permanence of the infected state, the virus survives in wild mice and is easily transmitted inadvertently by experimental procedures.

Keywords

Infected Mouse Newcastle Disease Virus Gamma Globulin Uninfected Mouse Plasma Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adams, D. H., and B. M. Bowiwn: An anti-virus action of azaserine-thioguanine in vivo. Nature (Lond.) 197, 316–317 (1963).CrossRefGoogle Scholar
  2. Adams, D. H., and B. M. Bowman: Studies on the properties of factors elevating the activity of mouse-plasma lactate dehydrogenase. Biochem. J. 90, 477–482 (1964).PubMedGoogle Scholar
  3. Adams, D. H., and E. J. Field: A plasma lactic dehydrogenase-elevating virus associated with scrapie-infected mice. J. gen. Virol. 1, 449–454 (1967).PubMedCrossRefGoogle Scholar
  4. Adams, D. H., K. E. K. Rowson, and M. H. Salaman: The effect of tumours, of leukaemia, and of some viruses associated with them, on the plasma lactic dehydrogenase activity of mice. Brit. J. Cancer 15, 860–867 (1961).PubMedCrossRefGoogle Scholar
  5. Allison, A. C.: Interference and interferon in relation to tumor viruses and tumor cells. In: Viruses, Nucleic Acids, and Cancer, pp. 462–484. Baltimore: Williams & Wilkins Co., 1963.Google Scholar
  6. Almeida, J. D., D. M. Berry, C. H. Cunningham, D. Hamre, M. S. Hofstad, L. Mallucci, K. Mcintosh, and D. A. J. Tyrrell: Coronaviruses. Nature (Loud.) 220, 650 (1968).Google Scholar
  7. Almeida, J. D., and C. A. Mims - The unique morphology of the lactic dehydrogenase agent. Microbios 10, 175–180 (1974).PubMedGoogle Scholar
  8. Almeida, J. D., and A. P. Waterson: The morphology of virus-antibody interaction. Advanc. Virus Res. 15, 307–338 (1969).CrossRefGoogle Scholar
  9. Amador, E., L. E. Dorfman, and W. E. C. Wacker: Serum lactic dehydrogenase activity; analytical assessment of current assays. Clin. Chem. 9, 391–399 (1963).Google Scholar
  10. Amador, E., H. Reinstein, and N. Benotti: Precision and accuracy of lactic dehydrogenase assays. Amer. J. clin. Path. 44, 62–70 (1965).Google Scholar
  11. Anderson, S. G., and G. L. Ada: Murray valley encephalitis virus: preparation of an infective “ribonucleic acid” fraction. Aust. J. exp. Biol. med. Sci. 37, 353–364 (1959).PubMedCrossRefGoogle Scholar
  12. Anderson, H. C., V. Riley, M. A. Fitzmaiirice, J. D. Loveless, P. Wade, and A. E. Moore: Quantitative study of the lactate dehydrogenase-elevating virus in mouse embryo cultures. J. nat. Cancer Inst. 36, 89–95 (1966).PubMedGoogle Scholar
  13. Anderson, H. C., V. Riley, P. Wade, and A. E. Moore: Quantitative evidence for propagation of the lactate dehydrogenase (LDH) elevating virus in mouse embryo cell cultures. Proc. Amer. Ass. Cancer Res. 6, 2 (1965).Google Scholar
  14. Andrewes, C. H., D. Blaskovic, J. B. Brooksby, J. Casals, H. S. Ginsberg, M. M. Kaplan, J. Maurin, J. L. Melnick, H. G. Pereira, R. Rott, P. Tournier, C. J. York, and V. Zhdanov: Generic names of viruses of vertebrates. Virology 40, 1070–1071 (1970).CrossRefGoogle Scholar
  15. Andrewes, C. H., and D. M. Horstmann: The susceptibility of viruses to ethyl ether. J. gen. Microbiol. 3, 290–297 (1949).PubMedGoogle Scholar
  16. Andrewes, C. H., and H. G. Pereira: Viruses of Vertebrates, 3rd Ed. London: Baillière Tindall, 1972.Google Scholar
  17. Ansari, K. A., C. F. Neilson, and P. G. Stansly: Pathogenesis of infectious splenic enlargement in mice. Exp. molec. Path. 2, 61–68 (1963).PubMedCrossRefGoogle Scholar
  18. Arison, R. N., J. A. Cassaro, and C. E. Shonk: Factors which affect plasma lactic dehydrogenase in tumor-bearing mice. Proc. Soc. exp. Biol. (N.Y.) 113, 497–501 (1963).Google Scholar
  19. Asada, M., and J. T. Galambos: Sorbitol dehydrogenase and hepatocellular injury: an experimental and clinical study. Gastroenterology 44, 578–587 (1963).Google Scholar
  20. Ashe, W. K. and A. L. Notkins: Neutralization of an infectious herpes simplex virus-antibody complex by anti-y-globulin. Proc. nat. Acad. Sci. (Wash.) 56, 447–451 (1966).CrossRefGoogle Scholar
  21. Asherson, G. L., and M. Bendinelli: Immunodepression by viruses: effect of Friend and Riley viruses on contact sensitivity. G. Microbiol. 17, 179–188 (1969).Google Scholar
  22. Bailey, J. M., J. Clough, and A. Lohaus: Influence of LDH virus on growth of Ehrlich ascites tumor in mice. Proc. Soc. exp. Biol. (N.Y.) 119, 1200–1204 (1965).Google Scholar
  23. Bailey, J. M., J. Clough, A. Lohaus, and D. A. Wright: A comparative study of LDH viruses from different tumors. Fed. Proc. 24, 597 (1965).Google Scholar
  24. Bailey, J. M., J. Clough, and M. Stearman: Plasma enzymes erythropoiesis and R.E.S. function in mice following infection with an LDH agent. Proc. Soc. exp. Biol. (N.Y.) 115, 642–646 (1964a).Google Scholar
  25. Bailey, J. M., J. Clough, and M. Stearman: Clearance of plasma enzymes in normal and LDH agent-infected mice. Proc. Soc. exp. Biol. (N.Y.) 117, 350–354 (1964b).Google Scholar
  26. Bailey, J. M., and M. Monroe: Studies on replication of LDH virus. Fed. Proc. 31, 836 (1972).Google Scholar
  27. Bailey, J. M., M. Stearman, and J. Clough: LDH levels in blood and tissues of mice infected with LDH agent. Proc. Soc. exp. Biol. (N.Y.) 114, 148–153 (1963).Google Scholar
  28. Bailey, J. M., and D. A. Wright: Plasma enzyme elevations with LDH viruses from different tumors. Proc. Soc. exp. Biol. (N.Y.) 120, 346–350 (1965).Google Scholar
  29. Baltimore, D.: Expression of animal virus genomes. Bact. Rev. 35, 235–241 (1971).PubMedGoogle Scholar
  30. Baron, S., C. E. Buckler, R. M. Friedman, and R. V. Mcclosizfy: Role of interferon during viraemia in mice. Bact. Proc. p. 116 (1964).Google Scholar
  31. Baron, S., C. E. Buckler, R. V. Mccloskey, and R. L. Kirschstein: Role of interferon during viraemia. 1. Production of circulating interferon. J. Immunol. 96, 12–16 (1966).PubMedGoogle Scholar
  32. Baron, S., H. G. Du Buy, C. E. Buckler, and M. L. Johnson: Relationship of interferon production to virus growth in vivo. Proc. Soc. exp. Biol. (N.Y.) 117, 338–341 (1964).Google Scholar
  33. Bayerle, H., A. Georgii und P. Jakob: Über das Verhalten des Lactatdehydrogenase aktivierenden Virus aus Mäusegeschwülsten bei der Autolyse. Z. Krebsforsch. 65, 171–172 (1962).CrossRefGoogle Scholar
  34. Bayerle, H., A. Georgii und K. E. Richard: Über die Aktivität von Serumfermenten nach zellfreier Beimpfung mit Ehrlich’schem Mäusetumorascites. Klin. Wschr. 40, 920 (1962).PubMedCrossRefGoogle Scholar
  35. Bell, R. L.: Separation of serum lactic dehydrogenase originating in myocardial and hepatic tissue, by means of heat fractionation. Amer. J. clin. Path. 40, 216–221 (1963).Google Scholar
  36. Bendinelli, M.: Conoscenze attuali sul virus di Riley o virus LDH. Ann. Sclavo 9, 253–280 (1967).Google Scholar
  37. Bendinelli, M., and G. L. Asherson: Depression of contact sensitivity by Friend and Riley viruses. Boll. Ist. sieroter. milan. 50, 502–507 (1971).PubMedGoogle Scholar
  38. Bierman, H. R., B. R. Hill, L. Reinhardt, and E. Emory: Correlation of serum lactic dehydrogenase activity with the clinical status of patients with cancer, lymphomas and the leukemias. Cancer Res. 17, 660–667 (1957).PubMedGoogle Scholar
  39. Bilbey, D. L. J., and T. Nicol: Effect of various natural steroids on the phagocytic activity of the reticuloendothelial system. Nature (Lond.) 182, 674 (1958).CrossRefGoogle Scholar
  40. Bladen, H. A., and A. L. Notkins: Electron microscopic demonstration of the lactic dehydrogenase agent. Virology 21, 269–271 (1963).PubMedCrossRefGoogle Scholar
  41. Borden, E. C., R. E. Shope, and F. A. Murphy: Physicochemical and morphological relationships of some arthropod-borne viruses to Bluetongue virus — A new taxonomic group. Physicochemical and serological studies. J. gen. Virol. 13, 261–271 (1971).PubMedCrossRefGoogle Scholar
  42. Boyd, J. W.: The rates of disappearance of L-lactate dehydrogenase isoenzymes from plasma. Biochim. biophys. Acta (Amst) 132, 221–231 (1967a).Google Scholar
  43. Boyd, J. W.: The disappearance of 14C-labelled isoenzyme 5 of L-lactate dehydrogenase. Biochim. biophys. Acta (Amst) 146, 590–593 (1967b).Google Scholar
  44. Boyd, J. W., and A. W. Phillips: Inhibition of Lymphoma 6C 3 HED by L-asparaginase from Serratia marcescens. J. nat. Cancer Inst. 46, 1271–1276 (1971).PubMedGoogle Scholar
  45. Brdiczha, D., A. Georgii und H. Zobl: Die Wirkung von Nucleinsäuren aus virushaltigen Mäusegeschwulsten auf die Lactatdehydrogenaseaktivität in Blutserum. Naturwissenschaften 50, 306–307 (1963).CrossRefGoogle Scholar
  46. Brier, A. M., C. Wohlenberg, J. Rosenthal, M. Mage, and A. L. Notkins: Inhibition or enhancement of immunological injury of virus infected cells. Proc. nat. Acad. Sci. (Wash.) 68, 3073–3077 (1971).CrossRefGoogle Scholar
  47. Broome, J. D.: Factors which may influence the effectiveness of L-asparaginases as tumor inhibitors. Brit. J. Cancer 22, 595–602 (1968).PubMedCrossRefGoogle Scholar
  48. 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
  49. Brutnner, K. T., D. Hurez, R. T. Mccloskey, and B. Benacerraf: Blood clearance of P32-labelled vesicular stomatitis and Newcastle disease viruses by the reticuloendothelial system in mice. J. Immunol. 85, 99–105 (1960).Google Scholar
  50. Burgess, E. A., and G. Sylvan: Lactic dehydrogenase activity in plasma and interstitial fluid during growth of mouse tumors. Cancer Res. 23, 714–719 (1963).PubMedGoogle Scholar
  51. Buscher, T. J., C. Frantsi, and K. F. Gregory: Fluctuating virus and enzyme levels in plasma of mice infected with Friend leukemia virus. Canad. J. Microhiol. 17, 315–321 (1971).Google Scholar
  52. Cahn, R. D., N. O. Kaplan, L. Levine, and E. Zwilling: Nature and development of lactic dehydrogenase. Science 136, 962–969 (1962).PubMedCrossRefGoogle Scholar
  53. Carver, D. H.: Personal communication (1969).Google Scholar
  54. Carver, D. H., P. I. Marcus, and D. S. Y. Seto: Intrinsic interference: a unique interference system used in assaying non-cytopathic viruses. Arch. ges. Virusforsch. 22, 55–60 (1967).CrossRefGoogle Scholar
  55. Cassels, A. C.: The release of lactate dehydrogenase from chick embryo cells infected with Semliki Forest virus. J. gen. Virol. 18, 203–205 (1973).CrossRefGoogle Scholar
  56. Cheng, P.-Y.: Infectivity of ribonucleic acid from mouse brains infected with Semliki forest virus. Nature (Lond.) 181, 1800 (1958).CrossRefGoogle Scholar
  57. Clough, J. D., and J. M. Bailey: Mechanism of plasma enzyme elevation by tumor LDH agent. Tex. Rep. Biol. Med. 23, 644–645 (1965).Google Scholar
  58. Commission on enzymes: Report International Union of Biochemistry. New York: Macmillan (Pergamon), 1961.Google Scholar
  59. Congdon, C. C.: Lymphatic tissue germinal centers in immune reactions. Progr. Biophys. molec. Biol. 19, 308–337 (1969). Oxford, England: Pergamon Press Ltd., 1969.Google Scholar
  60. Crispens, C. G.: Effect of storage on serum lactic dehydrogenase activity. Amer. Zool. 2, 515–516 (1962).Google Scholar
  61. Crispens, C. G.: Serum lactic dehydrogenase levels in mice during the development of autochthonous and chemically induced tumors. J. nat. Cancer Inst. 30, 361–366 (1963a).Google Scholar
  62. Crispens, C. G.: A lactic dehydrogenase elevating agent in association with human neoplasms. Nature (Lond.) 199, 1202–1203 (1963b).CrossRefGoogle Scholar
  63. Crispens, C. G.: Factors which influence normal values for serum lactic dehydrogenase in mice. Experientia (Basel) 19, 97–98 (1963c).CrossRefGoogle Scholar
  64. Crispens, C. G.: A preliminary report on attempts to demonstrate virus like entities in association with human neoplasms. Anat. Rec. 145, 314 (1963d).Google Scholar
  65. Crispens, C. G.: Preliminary studies on in utero transmission of the lactic dehydrogenase agent. Anat. Res. 149, 511 (1964a).Google Scholar
  66. Crispens, C. G.: On the epizootiology of the lactic dehydrogenase agent. J. nat. Cancer Inst. 32, 497–505 (1964b).Google Scholar
  67. Crispens, C. G.: Mouse plasma lactic dehydrogenase elevation: evidence for two particles. Virology 24, 501–502 (1964c).CrossRefGoogle Scholar
  68. Crispens, C. G.: The lactic dehydrogenase agent; its possible implications for the virologist and the oncologist. Bull. Sch. Med. Maryland 49, 7 (1964d).Google Scholar
  69. Crispens, C. G.: On the properties of the lactic dehydrogenase agent. J. nat. Cancer Inst. 35, 975–979 (1965a).Google Scholar
  70. Crispens, C. G.: On the transmission of the lactic dehydrogenase agent from mother to offspring. J. nat. Cancer Inst. 34, 331–336 (1965b).Google Scholar
  71. Crispens, C. G.: Properties of lactic dehydrogenase elevating agents. Anat. Rec. 151, 448–449 (1965c).Google Scholar
  72. Crispens, C. G.: Effect of actinomycin D on mice infected with lactate dehydrogenase virus. Experientia (Basel) 22, 823–824 (1966a).CrossRefGoogle Scholar
  73. Crispens, C. G.: Effect of thymectomy on mice infected with the lactate dehydrogenase agent. J. nat. Cancer Inst. 36, 81–87 (1966b).Google Scholar
  74. Crispens, C. G.: Association of the lactate dehydrogenase virus (Riley) with chemically induced murine neoplasms. Anat. Rec. 154, 456–457 (1966c).Google Scholar
  75. Crispens, C. G.: Lactate dehydrogenase virus and mouse embryos. Nature (Lond.) 214, 819 (1967a).CrossRefGoogle Scholar
  76. Crispens, C. G.: The lactate dehydrogenase virus: variations in the sex ratio of weanling mice. Anat. Rec. 157, 232 (1967b).Google Scholar
  77. Crispens, C. G.: Antibody response in normal and neonatally thymectomized mice infected with the lactate dehydrogenase virus. Anat Rec. 160, 466 (1968).Google Scholar
  78. Crispens, C. G.: Additional studies on the effect of the lactate dehydrogenase virus on murine sex ratios. Experientia (Basel) 25, 1197–1198 (1969).CrossRefGoogle Scholar
  79. Crispens, C. G.: Effect of statolon on lactate dehydrogenase virus infection in mice. Arch. ges. Virusforsch. 31, 191–195 (1970a).CrossRefGoogle Scholar
  80. Crispens, C. G.: Lactate dehydrogenase virus association with transplantable murine tumors. Experientia (Basel) 26, 891–892 (1970b).CrossRefGoogle Scholar
  81. Crispens, C. G.: Effect of the lactate dehydrogenase virus on the incidence of lymphocytic leukemia in C3H/Fg mice. Anat. Rec. 166, 294 (1970c).Google Scholar
  82. Crispens, C. G.: Studies on the response of SJL/J mice to infection with the lactate dehydrogenase virus. Arch. ges. Virusforsch. 35, 177–182 (1971).PubMedCrossRefGoogle Scholar
  83. Crispens, C. G.: Genetic control of the response of SJL/J mice to LDH virus infection. Arch. ges. Virusforsch. 38, 225–227 (1972).PubMedCrossRefGoogle Scholar
  84. Crispens, C. G., and T. A. Burns: Electronmicroscope investigation of lactic dehydrogenase agent. Nature (Lond.) 204, 1302 (1964).CrossRefGoogle Scholar
  85. Crispens, C. G., and I. F. Rey: Additional studies on the effect of neonatal thymectomy and lactate dehydrogenase virus infection on mice. Experientia (Basel) 23, 681–683 (1967).CrossRefGoogle Scholar
  86. Crispens, C. G., and W. K. Whitten: Strain differences in sex ratio response of mice to lactate dehydrogenase virus infection. Experientia (Basel) 27, 41–42 (1971).CrossRefGoogle Scholar
  87. Dalton, A. J., F. Haguenau, and J. B. Moloney: Morphology of particles associated with marine leukemia as revealed by negative staining: preliminary report. J. nat. Cancer Inst. 29, 1177–1178 (1962).PubMedGoogle Scholar
  88. Darnell, M. B., and P. G. W. Plagemann: Physical properties of lactic dehydrogenase-elevating virus and its ribonucleic acid. J. Virol. 10, 1082–1085 (1972).PubMedGoogle Scholar
  89. Darnell, M. B., and P. G. W. Plagemann: Replication of lactic dehydrogenaseelevating virus and its ribonucleic acid in peritoneal macrophage cultures. Abstr. ann Meet. Amer. Soc. Microbiol., p. 203 (1973).Google Scholar
  90. De Harven, E.: Viraemia in Friend murine leukemia: the electron microscope approach to the problem. Path. et Biol. 13, 125–134 (1965).Google Scholar
  91. De Harven, E., and C. Friend: Structure of virus particles partially purified from the blood of leukemic mice. Virology 23, 119–124 (1964).PubMedCrossRefGoogle Scholar
  92. De Harven, E., and C. Friend: Origin of the viremia in marine leukemia. Nat. Cancer Inst. Monogr. No. 22, 79–105 (1966).PubMedGoogle Scholar
  93. Dent, P. B.: Immunodepression by oncogenic viruses. Progr. med.Virol. 14, 1–35 (1972).Google Scholar
  94. De Thé, G., and A. L. Notmins: Ultrastructure of the lactic dehydrogenase virus (LDV) and cell-virus relationships. Virology 26, 512–516 (1965).CrossRefGoogle Scholar
  95. Dimmock, N. J., and D. A. J. Tyrrell: Some physico-chemical properties of rhino-viruses. Brit. J. exp. Path. 45, 271–280 (1964).PubMedGoogle Scholar
  96. Dreyfus, J.-CL., G. Scnapira, J. Demos: Etude de la créatine-kinase sérique chez les myopathes et leurs familles. Rev. franç. Etud. clin. biol. 5, 384–386 (1960).PubMedGoogle Scholar
  97. Dreyfus, J. C., G. Schapira, and F. Pira: Serum enzymes in the physiopathology of muscle. Ann N Y. Acad. Sci. 75, 235–249 (1958).PubMedCrossRefGoogle Scholar
  98. Du Buy H., S. Baron, C Uhlendorf, and M. L. Johnson: Role of interferon in murine lactic dehydrogenase virus infection, in vivo and in vitro. Infection and Immunity 8, 977–984 (1973).Google Scholar
  99. Du Buy H. G., and M. L. Johnson: Some properties of the lactic dehydrogenase agent of mice. J. exp. Med. 122, 587–600 (1965).PubMedCrossRefGoogle Scholar
  100. Du Buy H. G., and M. L. Johnson: Studies on the in vitro and in vivo multiplication of the LDH virus of mice. J. exp. Med. 123, 985–998 (1966).PubMedCrossRefGoogle Scholar
  101. Du Buy H. G., and M. L. Johnson: Further studies on the in vitro replication of lactic dehydrogenase virus in peritoneal macrophage cultures. Proc. Soc. exp. Biol. (N.Y.) 128, 1210–1214 (1968).Google Scholar
  102. Du Blet, H. G., and M. L. Johnson: Effect of actinomycin D on lactic dehydrogenase virus multiplication in mouse macrophages. Proc. Soc. exp. Biol. (N.Y.) 133, 1023–1025 (1970).Google Scholar
  103. Du Buy H. G., M. Worthington, AND M. L. Johnson: Effect of an immunosuppressive agent, cyclophosphamide on chronic lactic dehydrogenase virus viremia of mice. Infection and Immunity 4, 720–724 (1971).Google Scholar
  104. Ebert, P. S., M. A. Chirigos, and S. P. Chan: Studies on the enzymology of the rhabdomyosarcoma induced by the murine sarcoma virus (Moloney). Cancer Res. 30, 960–965 (1970).PubMedGoogle Scholar
  105. Ebert, P. S., M. A. Chirigos, and P. A. Ellsworth: Differential response of Friend leukemia virus and lactate dehydrogenase virus to chemotherapy and in vitro neutralization. Cancer Res. 28, 363–367 (1968).PubMedGoogle Scholar
  106. Ebert, P. S., M. A. Chirigos, L. A. Fields, and P. A. Ellsworth: Plasma lactate dehydrogenase and spleen heure biosynthetic activity following Friend and Rauscher leukemia virus infections. Life Sei. 6, 1963–1971 (1967).CrossRefGoogle Scholar
  107. Elliott, B. A., E. M. Jepson, and J. H. Wilkinson: Serum a-hydroxybutyrate dehydrogenase — A new test with improved specificity for myocardial lesions. Clin. Sci. 23, 305–316 (1962).Google Scholar
  108. Elliott, B. A., and J. H. Wilkinson: The serum “a-hydroxybutyrate dehydrogenase” in diseases other than myocardial infarction. Clin. Sci. 24, 343–355 (1963).Google Scholar
  109. Evans, R.: Replication of Riley’s plasma enzyme elevating virus in vitro. J. gen. Microbiol. 37, 7 (1964).Google Scholar
  110. Evans, R.: Replication of Riley’s plasma enzymes-elevating virus in tissue culture: the importance of the cellular composition. J. gen. Virol. 1, 363–374 (1967).PubMedGoogle Scholar
  111. Evans, R.: Factors affecting replication of the lactate dehydrogenase-elevating virus (LDH virus) in peritoneal macrophage. J. gen. Microbiol. 57, 11 (1969).Google Scholar
  112. Evans, R.: Further studies on the replication of the lactate dehydrogenase-elevating virus (LDH virus) in mouse peritoneal macrophage cultures. Proc. Soc. exp. Biol. (N.Y.) 133, 831–836 (1970).Google Scholar
  113. Evans, R., and V. Riley: Circulating interferon in mice infected with the lactate dehydrogenase-elevating virus. J. gen. Virol. 3, 449–452 (1968).PubMedCrossRefGoogle Scholar
  114. Evans, R., and M. H. Salaman: Studies on the mechanism of action of Riley virus. III. Replication of Riley’s plasma enzyme-elevating virus in vitro. J. exp. Med. 122, 993–1002 (1965).PubMedCrossRefGoogle Scholar
  115. Falke, D., und W. P. Rowe: Die Interferenz zwischen dem Polyoma-Virus und dem Stomatitis-vesicularis-Virus in der Maus. Arch. ges. Virusforsch. 15, 210–219 (1965).PubMedCrossRefGoogle Scholar
  116. Feldman, H. A., and S. S. Wang: Sensitivity of various viruses to chloroform. Proc. Soc. exp. Biol. (N.Y.) 106, 736–738 (1961).Google Scholar
  117. Fenner, F.: In: The Biology of Animal Viruses, Vol. 1, p. 30. New York-London: Academic Press, 1968.Google Scholar
  118. Field, E. J., and D. H. Adams: Riley virus in wild mice. Lancet 1, 868 (1968).PubMedCrossRefGoogle Scholar
  119. Fitzmaurice, M. A., V. Riley, and G. A. Santisteban: Biological synergism between the LDH-virus and Eperythrozoon coccoides: studies on the mechanism. Path. Et Biol. 20, 743–750 (1972).Google Scholar
  120. Fleisher, G. A., and K. G. Wakim: The fate of enzymes in body fluids — an experimental study. I. Disappearance rates of glutarnic-pyruvic transaminase under various conditions. J. Lab. clin. Med. 61, 76–85 (1963a).Google Scholar
  121. Fleisher, G. A., and K. G. Wakim: Fate of enzymes in body fluids — an experimental study. III. Disappearance rates of glutamic-oxalacetic transaminase II under various conditions. J. Lab. clin. Med. 61, 98–106 (1963b).Google Scholar
  122. Franseen, C. C., and R. Mclean: The phosphatase activity of tissues and plasma in tumors of bone. Amer. J. Cancer 24, 299–317 (1941).Google Scholar
  123. Frantsi, C., and K. F. Gregory: Reproduction of the lactate dehydrogenase-elevating (Riley) virus in mouse embryonic liver cell cultures. Virology 37, 145–148 (1969).PubMedCrossRefGoogle Scholar
  124. Friend, C., and F. Wnbleski: Lactic dehydrogenase activity of serum in mice with transplantable leukemia. Science 124, 173–174 (1956).PubMedCrossRefGoogle Scholar
  125. Georgii, A.: Die Aktivitätsänderung der Lactatdehydrogenase im Serum nach Infektion mit Geschwulstvirus der Maus als Regulationsstörung in vivo. Verh. dtsch. path. Ges. 46, 357–358 (1962).Google Scholar
  126. Georgii, A.: Über das Lactatdehydrogenase-erhöhende Virus in Laboratoriumsgeschwülsten. Klin. Wschr. 42, 559–563 (1964).PubMedCrossRefGoogle Scholar
  127. Georgii, A., H. Bayerle, D. Brdiczba und H. Zobl: Über ein die Lactatdehydrogenase im Serum aktivierendes Virus aus Geschwülsten der Maus. Z. Krebsforsch. 65, 334–341 (1963).PubMedCrossRefGoogle Scholar
  128. Georgii, A. und D. Brdiczba: Die Überlebenszeit des Lactatdehydrogenase-Agens aus Mäusegeschwülsten in Fibroblastenkulturen bei längerer Inkubation. Z. Krebsforsch. 66, 207–212 (1964).CrossRefGoogle Scholar
  129. Georgii, A., P. Goldbrunner und D. Brdiczba: Der Einfluß von p-Aminosalicylat bei der Nucleinsäureisolierung auf das Lactatdehydrogenase aktivierende Virus des Mäusetumors Serkon. I. Naturwissenschaften 51, 66 (1964).CrossRefGoogle Scholar
  130. Georg, A., M. Jäger, H. Kroth und H. Bayerle: Activitätsänderungen der Lactatdehydrogenase im Mäuseplasma durch Beimpfung mit virushaltigen Geschwulstfiltraten oder virushaltigen Gewebekulturen. Experientia (Basel) 18, 71–72 (1962).CrossRefGoogle Scholar
  131. Georg, A. und I. Kirschenhofer: Über die Isolierung von Lactat-Dehydrogenaseerhöhendem Virus aus wilden Mäusen. Z. Naturforsch. 20, 1310 (1965).Google Scholar
  132. Georgii, A., H. Kroth und H. Bayerle: Weitere Untersuchungen über die Aktivierung der Lactatdehydrogenase im Serum durch ein Geschwulstvirus der Maus. Klirr Wschr. 40, 363 (1962).CrossRefGoogle Scholar
  133. Georgii, A., and I. Lenz: Failure to propagate a lactic dehydrogenase-elevating agent from mice tumours in mice embryo cultures. Nature (Lond.) 202, 1228–1229 (1964).CrossRefGoogle Scholar
  134. Georgii, A., I. Lenz, and H. Zobel: Penetration of the placental barrier by the lactate dehydrogenase-elevating virus (Riley) and its behaviour in mouse embryo cultures following infection in utero. Proc. Soc. exp. Biol. (N.Y.) 117, 322–326 (1964).Google Scholar
  135. Georgii, A. und L. Thorn: Die Wirkung von Lactat-Dehydrogenase-erhöhendem Virus (Riley-Virus) bei Mäusen mit primären und transplantierten Carcinomen. Z. Krebsforsch. 67, 156–165 (1965).CrossRefGoogle Scholar
  136. Georgii, A., L. Thorn und H. Wrba: Die Replikation von Riley’s Enzym-erhöhendem Virus in embryonalen Mäusefibroblasten. Z. Naturforsch. 21, 298 (1966a).Google Scholar
  137. Georg, A., L. Thorn, and H. Wrba: Action of Riley’s enzyme-elevating virus on tumour-bearing mice. Nature (Loud.) 209, 929–930 (1966b).CrossRefGoogle Scholar
  138. Gevaudan, P., R. Gay, G. Arnaud: Etude sur l’activité de la transaminase glutamique-oxalacétique dans les cellules KB en culture normale et après inoculation avec un virus apparenté de la chorioméningite. Maroc méd. 435, 1033–1041 (1961).Google Scholar
  139. Gevaudan, P., G. Gevaudan, R. Gay, G. Arnaud: Etude sur l’activité de la transaminase glutamique-oxalacétique dans les cellules KB en cultures normale et après inoculation de polio virus. Maroc méd. 418, 219–229 (1960).Google Scholar
  140. Gibbs, A. J.: Comparison of bee chronic paralysis virus with mouse lactic dehydrogenase virus. J. gen. Virol. 5, 447–449 (1969).CrossRefGoogle Scholar
  141. Gibbs, A. J., B. D. Harrison, D. H. Watson, and P. Wildy: What’s in a virus name ? Nature (Lond.) 209, 450–454 (1966).CrossRefGoogle Scholar
  142. Gierer, A., and G. Schramm: Infectivity of ribonucleic acid from tobacco mosaic virus. Nature (Loud.) 177, 702–703 (1956).CrossRefGoogle Scholar
  143. Gilbert, V. E.: Enzyme release from tissue cultures as an indicator of cellular injury by viruses. Virology 21, 609–616 (1963).PubMedCrossRefGoogle Scholar
  144. Ginoza, W.: The effects of ionizing radiation on nucleic acids of bacteriophages and bacterial cells. Ann. Rev. Microbiol. 21, 325–368 (1967).CrossRefGoogle Scholar
  145. Giusti, G. und F. Piccinino: Beobachtungen über die Plasma-TriosephosphatIsomerase-Aktivität bei Lebererkrankungen. Acta hepato-splenol. (Stuttg.) 10, 166–175 (1963).Google Scholar
  146. Gledhill, A. W., D. L. J. Bilbey, and J. S. F. Niven: Effect of certain murine pathogens on phagocytic activity. Brit. J. exp. Path. 46, 433–442 (1965).PubMedGoogle Scholar
  147. Gledhill, A. W., and K. E. K. Rowson: Unpublished data (1965).Google Scholar
  148. Gottschalk, R. G., H. H. Grantham, and P. O. Miller: Serum lactate dehydrogenase of chickens with sarcoma 13. Cancer Res. 25, 919–921 (1965).PubMedGoogle Scholar
  149. Green, M.: Chemistry and structure of animal virus particles. Amer. J. Med. 38, 651–668 (1965).PubMedCrossRefGoogle Scholar
  150. Gutman, A. B.: Serum alkaline phosphatase activity in diseases of the skeletal and hepatobiliary systems. Amer. J. Med. 27, 875–901 (1959).PubMedCrossRefGoogle Scholar
  151. Gutman, A. B., and E. B. Gutmuan: An “acid” phosphatase occurring in the serum of patients with metastasizing carcinoma of the prostate gland. J. clin. Invest. 17, 473–478 (1938).PubMedCrossRefGoogle Scholar
  152. Halpern, B. N., G. Biozzi, T. Nicol, and D. L. J. Bilbey: Effect of experimental biliary obstruction on the phagocytic activity of the reticulo-endothelial system. Nature (Lond.) 180, 503–504 (1957).CrossRefGoogle Scholar
  153. Hanna, M. G., A. K. Szakal, and R. L. Tyndall: Histoproliferative effect of Rauscher leukemia virus on lymphatic tissue: histological and ultrastructural studies of germinal centers and their relation to leukemogenesis. Cancer Res. 30, 1748–1763 (1970).PubMedGoogle Scholar
  154. Hanna, M. G., H. E. Walburg, R. L. Tyndall, and M. J. Snodgrass: Histoproliferative effect of Rauscher leukemia virus on lymphatic tissue. II. Antigen-stimulated germfree and conventional BALB/c mice. Proc. Soc. exp. Biol. (N.Y.) 134, 1132–1141 (1970).Google Scholar
  155. Hill, B. R., and C. Levi: Elevation of a serum component in neoplastic disease. Cancer Res. 14, 513–515 (1954).PubMedGoogle Scholar
  156. Hill, B. R., and R. T. Jordan: Serum lactic dehydrogenase activity in mice with transplantable leukemia. Cancer Res. 17, 144–147 (1957).PubMedGoogle Scholar
  157. Hill, B. R., K. Tanaka, and E. Roberts: Elevation of plasma lactic dehydrogenase in mice receiving Moloney virus. Proc. Amer. Ass. Cancer Res. 3, 328 (1962).Google Scholar
  158. Hirsch, M. S., A. C. Allison, and J. J. Harvey: Immune complexes in mice infected neonatally with Moloney leukaemogenic and murine sarcoma virus. Nature (Lond.) 223, 739–740 (1969).CrossRefGoogle Scholar
  159. Hsieh, K. M., V. Suntzeff, and E. V. Cowdry: Comparative study of serum lactic dehydrogenase activity in mice with transplanted and induced tumors. Cancer Res. 16, 237–239 (1956).PubMedGoogle Scholar
  160. Horzinek, M. C.: Comparative aspects of togaviruses. J. gen. Virol. 20, Supplement, pp. 87–103 (1973).Google Scholar
  161. Horzinek, M., and M. Mussgay: Studies on the nucleocapsid structure of a group A arbovirus. J. Virol. 4, 514–520 (1969).PubMedGoogle Scholar
  162. Howard, R. J., A. L. Notkins, and S. E. Mergenhagen: Inhibition of cellular immune reactions in mice infected with lactic dehydrogenase virus. Nature (Lond.) 221, 873–874 (1969).CrossRefGoogle Scholar
  163. Isaacs, A.: Particle counts and infectivity titrations for animal viruses. Advanc.Virus Res. 4, 111–158 (1957).CrossRefGoogle Scholar
  164. Jacobson, K. B., and K. Nishio: Studies on plasma lactic dehydrogenase in mice with myeloid leukemia. II. On the site of production of the enzyme. Cancer Res. 23, 344–348 (1963).PubMedGoogle Scholar
  165. Kampschmidt, R. F., H. F. ÜPchurch, and H. L. Johnson: Plasma enzymes in tumor-bearing rats. Cancer Res. 26, 237–240 (1966).PubMedGoogle Scholar
  166. Karmen, A., F. Wrôblewski, and J. S. La Due: Transaminase activity in human blood. J. clin. Invest 34, 126–133 (1955).PubMedCrossRefGoogle Scholar
  167. Keir, H. M.: Virus-induced enzymes in mammalian cells infected with DNA-viruses. In: The Molecular Biology of Viruses, pp. 67–99, 18th Symp. Soc. gen. Microbiol. (L. V. Crawford and M. P. G. Stoker, eds.). Cambridge Univ. Press, 1968.Google Scholar
  168. Kekki, M., and A. Eisalo: Turnover of 35S-labelled serum albumin and gamma globulin in the rat: comparison of the resolution of plasma radioactivity curves by graphic means (manually) and by computer. Ann. Med. exp. Fenn. 42,196–208 (1964).PubMedGoogle Scholar
  169. Kelly, R., and D. Greiff: The level of lactic dehydrogenase activity as an indicator of the growth of influenza virus in the embryonate egg. J. exp. Med. 113, 125–129 (1961).PubMedCrossRefGoogle Scholar
  170. Kennedy, S. I. T., and D. C. Burre: Studies on the structural proteins of Semliki Forest virus. J. gen. Virol. 14, 87–98 (1972).PubMedCrossRefGoogle Scholar
  171. King, E. J.: Introductory remarks to the symposium. Amer. J. Med. 27, 849–860 (1959).CrossRefGoogle Scholar
  172. King, E. J., and D. M. Campbell: International enzyme units an attempt at international agreement. Clin. chim. Acta 6, 301–306 (1961).PubMedCrossRefGoogle Scholar
  173. King, E. J., and D. W. Moss: International enzyme units and isoenzyme nomenclature. J. clin. Path. 16, 391–393 (1963).CrossRefGoogle Scholar
  174. Latner, A. L., P. S. Gardner, D. M. Turner, and J. O. Brown: Effect of a possible oncogenic virus (adenovirus type 12) on lactate dehydrogenase in tissue culture. Lancet 1, 197–198 (1964).PubMedCrossRefGoogle Scholar
  175. Lea, D. E.: Actions of Radiations on living Cells. London-New York: Cambridge Univ. Press, 1946.Google Scholar
  176. Leader, R. W., and A. I. Hurvitz: Interspecies patterns of slow virus diseases. Ann. Rev. Med. 23, 191–200 (1972).PubMedCrossRefGoogle Scholar
  177. Levy, H. B., D. Axelrod, and S. Baron: Messenger RNA for interferon production. Proc. Soc. exp. Biol. (N.Y.) 118, 384–385 (1965).Google Scholar
  178. Levy, J. P., M. Bcirgn, D. Silvestre, and J. Bernard: The ultrastructure of Rauscher virus. Virology 26, 146–150 (1965).PubMedCrossRefGoogle Scholar
  179. Luria, S. E., R. C. Williams, and R. C. Backus: Electron micrographic counts of bacteriophage particles. J. Bact. 61, 179–188 (1951).PubMedGoogle Scholar
  180. Maeyer, E. De, and J. De Maeyer Guinguard: Contribution to U.I.C.C. Cancer Conference on “Cellular Control Mechanisms and Cancer”. Amsterdam, 1963.Google Scholar
  181. Mary, B. W. J.: Unpublished data (1963).Google Scholar
  182. Mary, B. W. J.: Action of Riley’s plasma enzyme-elevating virus in mice. Virology 24, 481–483 (1964).CrossRefGoogle Scholar
  183. Mary, B. W. J., J J Harvey, and K. E. K. Rowson: Some physical properties of a murine sarcoma virus (Harvey). Tex. Rep. Biol. Med. 24, 620–628 (1966).Google Scholar
  184. Mary, B. W. J., C. W Parr, and K. E. K. Rowson: Increased plasma isomerase and transaminase activity in mice infected with lactic dehydrogenase-elevating virus. Nature (Lond.) 198, 885 (1963a).CrossRefGoogle Scholar
  185. Mary, B. W. J., C. W. Parr, and K. E. K. Rowson: Plasma enzyme levels in mice infected with various viruses. J. gen. Microbiol. 32, 1 (1963b).Google Scholar
  186. Mary, B. W. J., and K. E. K. Rowson: Isoenzymic specificity of impaired clearance in mice infected with Riley virus. Science 149, 756–757 (1965).CrossRefGoogle Scholar
  187. Mary, B. W. J., K. E. K. Rowson, and C. W. Parr: Effect of Riley’s plasma enzyme-elevating virus (RV) on control of plasma enzyme levels in mice. Proc. biochem. Soc., Biochem. J. 95, 19–20P (1965).Google Scholar
  188. Mary, B. W. J., K. E. K. Rowson, and C. W. Parr: Studies on the mechanism of action of Riley virus. IV. The reticuloendothelial system and impaired plasma enzyme clearance in infected mice. J. exp. Med. 125, 277–288 (1967).CrossRefGoogle Scholar
  189. Mary, B. W. J., K. E. K. Rowson, C. W. Parr, and M. H. Salanian: Studies on the mechanism of action of Riley virus. I. Action of substances effecting the reticuloendothelial system on plasma enzyme levels in mice. J. exp. Med. 122, 967–981 (1965).CrossRefGoogle Scholar
  190. Mary, B. W. J., K. E. K. Rowson, M. H. Salaman, and C. W. Parr: Plasma enzyme levels in virus infected mice. Virology 23, 528–541 (1964).CrossRefGoogle Scholar
  191. Mary, B. W. J., and E. D. Wachsmute: Studies on the clearance of lactic dehydrogenase (LDH) isoenzymes from plasma of normal mice and mice infected with lactic dehydrogenase virus (LDV). J. med. Microbiol. 6, 98 (1973).Google Scholar
  192. Manso, C., K. Sugiura, and F. Wrblewsri: Glutathione reductase and lactic dehydrogenase activities of tissues of rodents with transplantable tumors. Cancer Res. 18, 682–686 (1958).PubMedGoogle Scholar
  193. Marcus, P. I., and D. H. Carver: Intrinsic interference: a new type of viral interference. J. Virol. 1, 334–343 (1967).PubMedGoogle Scholar
  194. Marcus, P. I., and D. H. Carver: Hemadsorption-negative plaque test for viruses inducing intrinsic interference. In: Fundamental Techniques inVirology, pp.161–183 (K. Habel and N. P. Salzman, eds.). New York-London: Academic Press, 1969.Google Scholar
  195. Massarrat, S: Enzyme kinetics, half-life, and immunological properties of iodine-131-labelled transaminases in pig blood. Nature (Lond.) 206, 508–509 (1965).CrossRefGoogle Scholar
  196. Melnick, J. L.: Classification and nomenclature of animal viruses. Progr. med. Virol. 13, 462–484 (1971).Google Scholar
  197. Mergenhagen, S. E., A. L. Noteins, and S. F. Dougherty: Adjuvanticity of lactic dehydrogenase virus: influence of virus infection on the establishment of immunologic tolerance to a protein antigen in adult mice. J. Immunol. 99, 576–581 (1967).PubMedGoogle Scholar
  198. Mericas, G., E. Anagnostou, ST Iiadziyannis, and S. Kaeari: The diagnostic value of serum leucine aminopeptidase. J. clin. Path. 17, 52–55 (1964).PubMedCrossRefGoogle Scholar
  199. Michaelides, M. C., and S. Schtfsinger: Structural proteins of lactic dehydrogenase virus. Virology 55, 211–217 (1973).PubMedCrossRefGoogle Scholar
  200. Melides, M. C., and S. Schlesinger: Effect of acute or chronic infection with lactic dehydrogenase virus (LDV) on the susceptibility of mice to plasmacytoma MOPC-315 J Immunol. 112, 1560–1564 (1974).Google Scholar
  201. Mims, C. A.: Aspects of the pathogenesis of virus diseases. Bact. Rev. 28, 30–71 (1964).PubMedGoogle Scholar
  202. Mundy, J., and P. C. Williams: Transmissible agent associated with some mouse neoplasms. Science 134, 834–835 (1961).PubMedCrossRefGoogle Scholar
  203. Nicol, T., D. L. J. Bilbey, J. Cordingley, and C. Druce: Response of the reticuloendothelial system to stimulation with oestrogens. Nature(Lond.) 192, 978–979 (1961).CrossRefGoogle Scholar
  204. Nicol, T., and D. L. J. Bilbey: Reversal by diethyl-stilboestrol of the depressant effect of cortisone on the phagocytic activity of the reticulo-endothelial system. Nature (Lond.) 179, 1137–1138 (1957).CrossRefGoogle Scholar
  205. Niwa, A., S. Yaniazaki, J. Bader, and A. L. Notgins: Incorporation of labelled precursors into RNA and protein of lactic dehydrogenase virus. J. Virol. 12, 401–404 (1973).PubMedGoogle Scholar
  206. Notkins, A. L.: Studies on the properties and transmission of the lactic dehydrogenase agent. Proc. Amer. Ass. Cancer Res. 4, 48 (1963a).Google Scholar
  207. Notkins, A. L.: Relationship between the multiplication of lactic dehydrogenase agent and plasma enzyme activity. Fed. Proc. 22, 487 (1963b).Google Scholar
  208. Notkins, A. L.: Recovery of an infectious ribonucleic acid from the lactic dehydrogenase agent by treatment with ether. Virology 22, 563–567 (1964a).CrossRefGoogle Scholar
  209. Notkins, A. L.: Recovery of an infectious nucleic acid from the lactic dehydrogenase agent by extraction with ether, chloroform or butanol. Fed. Proc. 23, 131 (1964b).Google Scholar
  210. Notkins, A. L.: Lactic dehydrogenase virus. Bact. Rev. 29, 143–160 (1965a).Google Scholar
  211. Notkins, A. L.: Studies on the mechanism of enzyme elevation in mice infected with the lactic dehydrogenase virus. Fed. Proc. 24, 378 (1965b).Google Scholar
  212. Noteins, A. L.: Recovery of an infectious ribonucleic acid from the lactic dehydrogenase virus following extraction with butanol or chloroform. Biochim. biophys. Acta (Amst) 103, 509–511 (1965c).Google Scholar
  213. Notkins, A. L.: Infectious virus-antibody complexes during chronic viremia. Proc. 9th Int. Cancer Congr., Tokyo, p. 310 (1966a).Google Scholar
  214. Notkins, A. L.: Catabolism of y-globulin and increased antibody production in mice infected with lactic dehydrogenase virus. Proc. 9th Int. Congr. Microbiol., p. 628, Moscow, 1966b.Google Scholar
  215. Notkins, A. L.: Infectious virus-antibody complex. Fed. Proc. 25, 615 (1966c).Google Scholar
  216. Noteins, A. L.: Neutralization of sensitized virus by anti-gammaglobulin. Perspect. Virol. 6, 189–192 (1968).Google Scholar
  217. Notkins, A. L: Enzymatic and immunologic alterations in mice infected with lactic dehydrogenase virus. Amer. J. Path. 64, 733 746 (1971a).Google Scholar
  218. Notkins, A. L.: Infectious virus-antibody complexes-interaction with anti-immunoglobulins, complement, and rheumatoid factor. J. exp. Med. 134, 41s-51s (1971b).Google Scholar
  219. Notkins, A. L., R. J. Berry, J. B. Moloney, and R. E. Greenfield: Relationship of the lactic dehydrogenase factor to certain murine tumors. Nature (Lond.) 193, 79–80 (1962).CrossRefGoogle Scholar
  220. Notkins, A. L., and M. Cosmides: The effect of heparin on the titer of the infectious nucleic acid from the lactic dehydrogenase agent. Biochim. biophys. Acta (Amst.) 91, 536–538 (1964).Google Scholar
  221. Notkins, A. L., and R. E. Greenfield: Infection of tumor-bearing mice with the lactic dehydrogenase agent. Proc. Soc. exp. Biol. (N.Y.) 109, 988–991 (1962a).Google Scholar
  222. Notkins, A. L., and R. E. Greenfield: The lactic dehydrogenase factor in the tumorbearing animal. Proc. Amer. Ass. Cancer Res. 3, 348 (1962b).Google Scholar
  223. Notkins, A. L., R. E. Greenfield, D. Marshall, and L. Bane: Multiple enzyme changes in the plasma of normal and tumor-bearing mice following infection with the lactic dehydrogenase agent. J. exp. Med. 117, 185–195 (1963).PubMedCrossRefGoogle Scholar
  224. Notkins, A. L., M. Mage, W. K. Ashe, and S. Mahar: Neutralization of sensitized lactic dehydrogenase virus by anti-y-globulin. J. Immunol. 100, 314–320 (1968).PubMedGoogle Scholar
  225. Notkins, A. L., S. Mahar, C Scheele, and J. Goffman: Infectious virus-antibody complex in the blood of chronically infected mice. J. exp. Med. 124, 81–97 (1966).PubMedCrossRefGoogle Scholar
  226. Notkins, A. L., S. E. Mergenhagen, and R. J. Howard: Effect of virus infections on the function of the immune system. Ann. Rev. Microbiol. 24, 525–538 (1970).CrossRefGoogle Scholar
  227. Notins, A. L., S. E. Mergenhagen, A. A. Rizzo, C. Scheele, and T. A. Waldmann: Elevated y-globulin and increased antibody production in mice infected with lactic dehydrogenase virus. J. exp. Med. 123, 347–364 (1966).CrossRefGoogle Scholar
  228. Notkins, A. L., and C. Scheele: An infectious nucleic acid from the lactic dehydrogenase agent. Virology 20, 640–642 (1963a).CrossRefGoogle Scholar
  229. Notkins, A. L., and C. Scheele: Studies on the transmission and the excretion of the lactic dehydrogenase agent. J. exp. Med. 118, 7–12 (1963b).CrossRefGoogle Scholar
  230. Notkins, A. L., and C. Scheele: Impaired clearance of enzymes in mice infected with the lactic dehydrogenase agent. J. nat. Cancer Inst. 33, 741–749 (1964).PubMedGoogle Scholar
  231. Notkins, A. L., C. Scheele, and H. W. Scafmp: Transmission of the lactic dehydrogenase agent in normal and partially edentulous mice. Nature (Lond.) 202, 418–419 (1964).CrossRefGoogle Scholar
  232. Notkins, A. L., and S. J. Shochat: Studies on the multiplication and the properties of the lactic dehydrogenase agent. J. exp. Med. 117, 735–747 (1963).PubMedCrossRefGoogle Scholar
  233. Old, L. J., B. Benacerraf, D. A. Clarne, E. A. Carswell, and E. Stockert: The role of the reticuloendothelial system in the host reaction to neoplasia. Cancer Res. 21, 1281–1301 (1961).PubMedGoogle Scholar
  234. Old, L. J., C. Iritani, E. Stockert, E. A. Boyse, and H. A. Campbell: Increased antileukemic activity of E. coli asparaginase in mice infected with L.D.H.-elevating virus. Lancet 11, 684–685 (1968).CrossRefGoogle Scholar
  235. Oldstone, M. B. A., and F. J. Dixon: Pathogenesis of chronic disease associated with persistant lymphocytic choriomeningitis viral infection. J. exp. Med. 129, 483–505 (1969).PubMedCrossRefGoogle Scholar
  236. Oldstone, M. B. A., and F. J. Dixon: Inhibition of antibodies to nuclear antigen and to DNA in New Zealand mice infected with lactate dehydrogenase virus. Science 175, 784–786 (1972).PubMedCrossRefGoogle Scholar
  237. Oldstone, M. B. A., and F. J. Dixon: Lactic dehydrogenase virus-induced immune complex type of glomerulonephritis. J. Immunol. 106, 1260–1263 (1971).PubMedGoogle Scholar
  238. Oldstone, M. B. A., A. Tisnon, and J. M. Chiller: Chronic virus infection and immune responsiveness. II. Lactic dehydrogenase virus infection and immune response to non-viral antigens. J. Immunol. 112, 370–375 (1974).PubMedGoogle Scholar
  239. Oldstone, M. B. A., S. Yamazaki, A Niwa, and A. L. Notkins: In vitro detection of cells infected with lactic dehydrogenase virus (LDV) by fluorescein-labelled antibody to LDV. Intervirology 2, 261–265 (1974).PubMedCrossRefGoogle Scholar
  240. Phillips, A., and J. Boyd: Blood clearance of asparaginase and tumor inhibition in mice infected with the lactic dehydrogenase-elevating virus. Bact. Proc., p. 153 (1969).Google Scholar
  241. Plagemann, P. G. W., K. F. Gregory, H. E. Swim, and K. K. W. Chan: Plasma lactic dehydrogenase-elevating agent of mice: distribution in tissues and effect on lactic dehydrogenase isozyme patterns. Canad. J. Microbiol. 9, 75–86 (1963).CrossRefGoogle Scholar
  242. Plagemann, P. G. W., and H. E. Swim: Studies of virus associated with metabolic disease in mice. Proc. 8th Int. Congr. Microbiol., p. 91, Montreal, 1962.Google Scholar
  243. Plagemann, P. G. W., and H. E. Swim: Studies of the plasma lactic dehydrogenase- elevating virus (PLDEV) of mice. Proc. Amer. Ass. Cancer Res. 4, 53 (1963).Google Scholar
  244. Plagemann, P. G. W., and H. E. Swml: Propagation of lactic dehydrogenase-elevating virus in cell culture. Proc. Soc. exp. Biol. (N.Y.) 121, 1147–1152 (1966a).Google Scholar
  245. Plage Mann, P. G. W., and H. E. Swim: Relationship between the lactic dehydrogenaseelevating virus and transplantable mucine tumors. Proc. Soc. exp. Biol. (N.Y.) 121, 1142–1146 (1966b).Google Scholar
  246. Plageann, P. G. W., M. Watanabe, and H. E. Swrm: Plasma lactic dehydrogenaseelevating agent of mice: effect on levels of additional enzymes. Proc. Soc. exp. Biol. (N.Y.) 111, 749–754 (1962).Google Scholar
  247. Polson, A., and M. H. V. Van Regenmortel: A new method for determination of sedementation constants of viruses. Virology 15, 397–403 (1961).PubMedCrossRefGoogle Scholar
  248. Pope, J. H.: Studies of a virus isolated from a wild house mouse, mus musculus, and producing splenomegaly and lymph node enlargement in mice. Aust. J. exp. Biol. med. Sci. 39, 521–536 (1961).PubMedCrossRefGoogle Scholar
  249. Pope, J. H.: Detection of an avirulent virus apparently related to Friend virus. Aust. J. exp. Biol. med. Sci. 41, 349–362 (1963).PubMedCrossRefGoogle Scholar
  250. Pope, J. H., and W. P. Rowe: Identification of WMI as LDH virus, and its recovery from wild mice in Maryland. Proc. Soc. exp. Biol. (N.Y.) 116, 1015–1019 (1964).Google Scholar
  251. Porter, D. D.: Quantitative view of the slow virus landscape. Progr. med. Virol. 13, 339–372 (1971).Google Scholar
  252. Porter, D. D., and H. G. Porter: Deposition of immune complexes in the kidneys of mice infected with lactic dehydrogenase virus. J. Immunol. 106, 1264–126 (1971).PubMedGoogle Scholar
  253. Porter, D. D., H. G. Porter, and B. B. Deerhaxe: Immunofluorescence assay for antigen and antibody in lactic dehydrogenase virus infection of mice. J. Immunol. 102, 431–436 (1969).PubMedGoogle Scholar
  254. Proffitt, M. R., and C. C. Congdon: The effect of a large dose of LDH virus on mouse lymphatic tissue. Fed. Proc. 29, 559 (1970).Google Scholar
  255. Proffitt, M. R., C. C. Congdon, and R. L. Tyndall: The combined action of Rauscher leukemia virus and lactic dehydrogenase virus on mouse lymphatic tissue. Int. J. Cancer 9, 193–211 (1972).PubMedCrossRefGoogle Scholar
  256. Prosser, P. R., and R. Evans: An electron microscopic study of lactic dehydrogenase virus in cultures of mouse peritoneal macrophages. J. gen. Virol. 1, 419–424 (1967).PubMedCrossRefGoogle Scholar
  257. Rauen, H. M. und H. Hupe: Das Lactatdehydrogenase-Agens im Blute tumortragender Mäuse. Arzneimittel-Forsch. 13, 933–936 (1963).Google Scholar
  258. Reichard, H.: Ornithine carbamyl transferase activity in human serum in diseases of the liver and the biliary system. J. Lab. clin. Med. 57, 78–87 (1961).PubMedGoogle Scholar
  259. Richter, A., and E. Wecker: The reaction of EEE virus preparations with sodium deoxycholate. Virology 20, 263–268 (1963).PubMedCrossRefGoogle Scholar
  260. Riley, V.: Adaptation of orbital bleeding technic to rapid serial blood studies. Proc. Soc. exp. Biol. (N.Y.) 104, 751–754 (1960).Google Scholar
  261. Riley, V.: Virus-tumor synergism. Science 134, 666–668 (1961).PubMedCrossRefGoogle Scholar
  262. Riley, V.: Synergistic glycolytic activity associated with transmissible agents and neoplastic growth. J. gen. Physiol. 45, 614A–615A (1962a).Google Scholar
  263. Riley, V.: Role of viruses in glycolysis of tumors and hosts. Fed. Proc., pp. 21–87 (1962b).Google Scholar
  264. Riley, V.: Evidence for a minute infectious entity. Proc. Amer. Ass. Cancer Res. 4, 57 (1963a).Google Scholar
  265. Riley, V: Enzymatic determination of transmissible replicating factors associated with mouse tumors. Ann. N.Y. Acad. Sci. 100, 762–789 (1963b).Google Scholar
  266. Riley, V.: Transmissible agents and anaemia of mouse cancer. N.Y. State J. Med. 63, 1523–1531 (1963c).Google Scholar
  267. Riley, V.: Synergistic glycolytic activity associated with transmissible agents and neoplastic growth. In: Control Mechanisms in Respiration and Fermentation, pp. 211–241 (Barbara Wright, ed.). New York: Ronald Press, 1963d.Google Scholar
  268. Riley, V.: Synergism between a lactate dehydrogenase-elevating virus and Eperythrozoon coccoides. Science 146, 921–923 (1964).PubMedCrossRefGoogle Scholar
  269. Riley, V.: Discussion following a paper by Pollard, M., on “Neoplasia in germ-free animals” Perspect. Virol. 4, 265 (1965).Google Scholar
  270. Rrrey, V.: Spontaneous mammary tumors: decrease of incidence in mice infected with an enzyme-elevating virus. Science 153, 1657–1658 (1966a).CrossRefGoogle Scholar
  271. Riley, V.: Le virus elevant le taux de la deshydrogenase lactique. Thesis monograph University of Paris (1966b).Google Scholar
  272. Rufy, V.: Role of the LDH-elevating virus in leukemia therapy by asparaginase. Nature (Lond.) 220, 1245–1246 (1968a).Google Scholar
  273. Rirmy, V.: Lactate dehydrogenase in the normal and malignant state in mice and the influence of a benign enzyme-elevating virus. In: Methods in Cancer Research (Harris Busch, ed.) 4, 493–618, 1968b, Academic Press.Google Scholar
  274. Riley, V.: Asparaginase therapy: influence of the LDH-virus. Proc. Amer. Ass. Cancer Res. 10, 73 (1969).Google Scholar
  275. Riley, V.: Influence of a benign virus upon mouse leukemia during asparaginase therapy. Path. et Biol. 18, 757–764 (1970).Google Scholar
  276. Riley, V.: Rescue of an eclipsed LDH-virus by host immunosuppression techniques. Fed. Proc. 30, 1100 (1971).Google Scholar
  277. Riley, V.: Persistence and other characteristics of the lactate-dehydrogenase-elevating virus (LDH-virus). Progr. med. Virol. 18, 198–213 (1974a).Google Scholar
  278. Riley, V.: Biological contaminants and scientific misinterpretations (viruses). Cancer Res. 34, 1752–1754 (1974b).Google Scholar
  279. Riley, V.: Erroneous interpretation of valid experimental observations through interference by the LDH virus. J. nat. Cancer Inst. 52, 1673–1677 (1974c).Google Scholar
  280. Riley, V., H. A. Campbell, J. D. Loveless, and M. A. Fitzmaurice: Density gradient centrifugation and molecular sieve studies of lactic dehydrogenaseelevating virus-like agent. Proc. Amer. Ass. Cancer Res. 5, 53 (1964).Google Scholar
  281. Riley, V., H. A. Campbell, and C. C. Stock: Asparaginase clearance: influence of the LDH-elevating virus. Proc. Soc. exp. Biol. (N.Y.) 133, 38–42 (1970).Google Scholar
  282. Riley, V. and M. A. Fitzmaurice: “Helper” influence of the LDH-virus in the production of leukaemia by attenuated Rauscher virus. Proc. Amer. Ass. Cancer Res. 14, 112 (1973).Google Scholar
  283. Riley, V., M. A. Fitzmaurice, J. D. Loveless, T. G. Kryzab, M R Gallagher, and W. M. Siler: Mechanism of plasma enzyme elevation observed with virus infection and neoplastic growth. Proc. Amer. Ass. Cancer Res. 6, 54 (1965).Google Scholar
  284. Riley, V., E. Huerto, D. Bardell, M. A. Fitzmaurice, and J. D. Loveless: Studies on the origin of elevated plasma lactic dehydrogenase (LDH). Fed. Proc. 22, 242 (1963).Google Scholar
  285. Riley, V., E. Huerto, D. Bardell, J. D. Loveless, and M. A. Fitzmadbice: Influence of LDH-elevating virus on normal and tumor-bearing hosts. Proc. Amer. Ass. Cancer Res. 3, 354 (1962).Google Scholar
  286. Riley, V., E. Huerto, J. D. Loveless, D. Bardell, M. Fitzmaurice, and C. Forman: Inapparent transmissible agents in oncology and their influence on tumor and host. Acta Un. int. Caner. 19, 263–270 (1963).Google Scholar
  287. Riley, V., E. Huerto, F. Lilly, D. Bardell, J. D. Loveless, and M. A. Fitzmaurice: Some characteristics of virus-like entities associated with 30 varieties of experimental tumor. Proc. Amer. Ass. Cancer Res. 3, 262 (1961).Google Scholar
  288. Riley, V., F. Lilly, E. Huerto, and D. Bardell: Transmissible agent associated with 26 types of experimental mouse neoplasms. Science 132, 545–547 (1960).PubMedCrossRefGoogle Scholar
  289. Riley, V., J. D. Loveless, and M. A. Fitzmaurice: Comparison of a lactate dehydrogenase elevating virus-like agent and Eperythrozoon coccoides. Proc. Soc. exp. Biol. (N.Y.) 116, 486–490 (1964).Google Scholar
  290. Riley, V., J. D. Loveless, M. A. Fitzmaurice, and W. M. Siler: Mechanism of lactate dehydrogenase (LDH) elevation in virus infected hosts. Life Sci. 4, 487–507 (1965).PubMedCrossRefGoogle Scholar
  291. Riley, V., J. D. Loveless, M. A. Fitzmaurice, I. Smdllyan, and S. W. Fischer: Characteristics of the Friend’s leukemia disease in the presence and absence of a benign enzyme-elevating (LDH) virus. Proc. Amer. Ass. Cancer Res. 8, 56 (1967).Google Scholar
  292. Riley, V. and D. Specrman: Influence of the LDH-virus on the neoplastic process. XI Int. Cancer Congr. Abst. p. 676 (1974).Google Scholar
  293. Riley, V., D. H. Speckman, and M. A. Fitzmaurice: Influence of asparaginase and glutaminase upon free amino acids in normal and tumor-bearing mice. Colloques Internationaux C.N.R.S., No. 197, pp. 139–158 (1970a).Google Scholar
  294. Riley, V., D. H. Speckman, and M. A. Fitzmaurice: Critical influence of an enzyme-elevating virus upon long-term remissions of mouse leukemia following asparaginase therapy. Recent Results in Cancer Res. 33, 81–101 (1970b).Google Scholar
  295. Riley, V., D. H. Speckman, M. A. Fitzmaurice: Influence of the LDH-elevating virus in revealing profound alterations in host physiology during asparaginase therapy. Proc. Amer. Ass. Cancer Res. 12, 64 (1971).Google Scholar
  296. Riley, V., D. H. Speckman, M. A. Fitzmaurice, J. Roberts, J. S. Holcenberg, and W. C. Dolowy: Studies on a new glutaminase/asparaginase: therapeutic properties, half life, and alterations in the plasma amino acids. Proc. Amer. Ass. Cancer Res. 13, 117 (1972).Google Scholar
  297. Riley, V., D. H. Speckman, M. A. Fitzmaurice, J. Roberts, J. S. Holcenberg, and W. C. Dolowy: Therapeutic properties of a new glutaminase-asparaginase preparation and the influence of the lactate dehydrogenase-elevating virus. Cancer Res. 34, 429–438 (1974).PubMedGoogle Scholar
  298. Riley, V., D. H. Speckman, M. A. Fitzmaurice, and C. N. Lulham: Possible mechanism for permanent remissions of leukemia in mice treated with L-asparaginase. Xth Int. Cancer Congr. Proc., pp. 445–446 (1970).Google Scholar
  299. Rttfy, V., and F. Wrblewskt: Serial lactic dehydrogenase activity in plasma of mice with growing or regressing tumors. Science 132, 151–152 (1960).CrossRefGoogle Scholar
  300. Roberts, W. M.: Variations of the phosphatase activity of the blood in disease. Brit. J. exp. Path. 11, 90–95 (1930).Google Scholar
  301. Roberts, W. M.: Blood phosphatase and the van den Bergh reaction in the differentiation of the several types of jaundice. Brit. Med. J. 1, 734–738 (1933).PubMedCrossRefGoogle Scholar
  302. Roe, F. J. C., and K. E. K. Rowson: The induction of cancer by combinations of viruses and other agents. Int. Rev. exp. Path. 6, 181–227 (1968).PubMedGoogle Scholar
  303. Rose, A., M. West, and H. J. Zimmerman: Serum enzymes in disease. V. Isocitric dehydrogenase, malic dehydrogenase and glycolytic enzymes in patients with carcinoma of the breast. Cancer 14, 726–733 (1961).PubMedCrossRefGoogle Scholar
  304. Rowe, W. P.: Resistance of mice infected with Moloney leukemia virus to Friend virus infection. Science 141, 40–41 (1963).PubMedCrossRefGoogle Scholar
  305. Rowe, W. P., J. W. Hartley, and R. J. Huebner: Polyoma and other indigenous mouse viruses. In: The Problems of Laboratory Animal Diseases (R. J. C. Harris, ed.), pp. 131–142. London-New York: Academic Press, 1962.Google Scholar
  306. Rowe, W. P., F. A. Murphy, G. H. Bergold, J. Casals, J. Hotchin, K. M. Johnson, F Lehmanngrube, C. A. Mims, E. Traub, and P. A. Webb: Arenoviruses: proposed name for a newly defined virus group. J. Virol. 5, 651–652 (1970).PubMedGoogle Scholar
  307. Rowson, K. E. K.: Transmission of RV from parents to offspring. Brit. Emp Cancer Campaign Ann Rep. 40, 205–206 (1962).Google Scholar
  308. Rowson, K. E. K.: Riley virus in wild mice, effect of drugs on replication of Riley viruses. Brit. Emp Cancer Campaign Ann. Rep. 41, 222–223 (1963).Google Scholar
  309. Rowson, K. E. K.: Unpublished data (1964).Google Scholar
  310. Rowson, K. E. K.: Host range of RV. Brit. Emp. Cancer Campaign Ann. Rep. 44, 113 (1966).Google Scholar
  311. Rowson, K. E. K.: Decreased viraemia following injection of statalon. International Virology 1, 128, Basel: S. Karger, 1969.Google Scholar
  312. Rowson, K. E. K., D. H. Adams, and M. H. Salaman: Riley’s enzyme-elevating virus; a study of the infection in mice and its relation to virus-induced leukemia. Acta Un. in Caner. 19, 404–406 (1963).Google Scholar
  313. Rowson, K. E. K., and R. W. Horne: Unpublished data (1962).Google Scholar
  314. Rowson, K. E. K., and L. Michaels: Lactic dehydrogenase (LDH) virus and its localisation by immunofluorescence. J. med. Microbiol. 6, 10 (1973).Google Scholar
  315. Rowson, K. E. K., and B. W. J. Many: The interaction between Riley’s plasma enzyme elevating virus and the reticuloendothelial system. J. gen. Microbiol. 39, 11 (1965).Google Scholar
  316. Rowson, K. E. K., B. W. J. Mary, and M. Bendi Belli: Riley virus neutralizing activity in the plasma of infected mice with persistent viraemia. Virology 28, 775–778 (1966).PubMedCrossRefGoogle Scholar
  317. Rowson, K. E. K., B. W. J. Mary, and R. Eans: Site of Riley virus replication, and the source of the excess plasma enzymes in infected mice. Brit. Emp Cancer Campaign Ann. Rep. 41, 227 (1963).Google Scholar
  318. Rowson, K. E. K., B. W J Mary, and M. H. Salaman: Size estimation by filtration of the enzyme-elevating virus of Riley. Life Sci. 2, 479–485 (1963).CrossRefGoogle Scholar
  319. Rowson, K. E. K., B. W J Mary, and M. H. Salaman: Studies on the mechanism of action of Riley virus. II. Action of substances affecting the reticuloendothelial system on the level of viraemia. J. exp. Med. 122, 983–992 (1965).PubMedCrossRefGoogle Scholar
  320. Rowson, K. E. K., L. Michaels, and G. A. Hurst: Early changes in the kidneys of BALB/c mice infected with lactic dehydrogenase virus. Nature (Lond.) 248, 686–687 (1974).CrossRefGoogle Scholar
  321. Rowson, K. E. K., I. B. Parr, and T. Alper: The radiation target size of Riley virus infectivity. J. gen. Microbiol. 50, 11 (1968a).Google Scholar
  322. Rowson, K. E. K., I. B. Parr, and T. Alper: Radiation target size of Riley virus. Virology 36, 157–159 (1968b).CrossRefGoogle Scholar
  323. Rutenburg, A. M., J. A. Goldbarg, and E. P. Pineda: Serum y-glutamyl trans-peptidase activity in hepatobiliary pancreatic disease. Gastroenterology 45, 43–48 (1963).Google Scholar
  324. Salaman, M. H.: Immunodepression by viruses. Antibot. et Chemother. 15, 393–406 (1969).Google Scholar
  325. Salaman, M H: Immunodepression by mammalian viruses and plasmodia. Proc. roy. Soc. Med. 63, 11–15 (1970).PubMedGoogle Scholar
  326. Salaman, M. H., and N. Wedderburn: The immunodépressive effect of Friend virus. Immunology 10, 445–458 (1966).Google Scholar
  327. Salem, H., M. H. Grossman, and D. L. J. Bilbey: Micro-method for intravenous injection and blood sampling. J. pharm. Sci. 52, 794–795 (1963).PubMedCrossRefGoogle Scholar
  328. Salthe, S. N., O. P. Chzlson, and N. O. Kaplan: Hybridization of lactic dehydrogenase in vivo and in vitro. Nature (Lond.) 207, 723–726 (1965).CrossRefGoogle Scholar
  329. Santisteban, G. A., V. Riley, and M. A. Fitzmaurice: Thymolytic and adrenal cortical responses to the LDH-elevating virus. Proc. Soc. exp. Biol. (N.Y.) 139, 202–206 (1972).Google Scholar
  330. Santisteban, G. A., V. Riley, and K. Willhight: Studies in virus-tumor relationships: responses of the adrenocortical-thymolymphatic system to the LDH-elevating virus. Abstracts, Tenth Int. Cancer Congr., p. 302. Medical Arts Publishing Co., Austin, 1970.Google Scholar
  331. Schaffer, F. L.: Physical and chemical properties and infectivity of RNA from animal viruses. Cold Spr. Harb. Symp. quant. Biol. 27, 89–99 (1962).Google Scholar
  332. Schapira, F.; J.-C. Dreyfus, G. Schapira: La durée de séjour dans le plasma de l’aldolase chez le lapin: étude à l’aide d’une aldolase marquée à l’iode radioactif. Rev. franç. Études clin. biol. 7, 829–832 (1962).PubMedGoogle Scholar
  333. Schwartz, M. A., M. West, W. S. Walsh, and H. J. Zimmerman: Serum enzymes in disease. VIII. Glycolytic and oxidative enzymes and transaminases in patients with gastrointestinal carcinoma. Cancer 15, 346–353 (1962).CrossRefGoogle Scholar
  334. Sibley, J. A., and A. L. Lehninger: Aldolase in the serum and tissues of tumor-bearing animals. J. nat. Cancer Inst. 9, 303–309 (1949a).Google Scholar
  335. Sibley, J. A., and A. L. Lehninger: Determination of aldolase in animal tissues. J. biol. Chem. 177, 859–872 (1949b).Google Scholar
  336. Snodgrass, M. J., and M. G Hanna: Histoproliferative effect of Rauscher leukemia virus on lymphatic tissue. III. Alterations in the thymic-dependent area induced by the passenger lactic dehydrogenase virus. J. nat. Cancer Inst. 45, 741–759 (1970).PubMedGoogle Scholar
  337. Snodgrass, M. J., D. S. Lowrey, and M. G. Hanna: Changes induced by lactic dehydrogenase virus in thymus and thymus-dependent areas of lymphatic tissue. J. Immunol. 108, 877–892 (1972).PubMedGoogle Scholar
  338. Snodgrass, M. J., J. M. Yuhas, and M. G. Hanna: Histoproliferative effect of Rauscher leukemia virus on lymphatic tissues. IV. Lactic dehydrogenase virus and erythropoietin potentiation of the erythroid response. J. nat. Cancer Inst. 50, 735–743 (1973).PubMedGoogle Scholar
  339. Speckman, D., and V. Riley: E-N-Monomethyllysine and other plasma amino acids in leukemic mice and effects of asparaginase. Fed. Proc. 30, 1067 (1971).Google Scholar
  340. Speckman, D., and V. Riley: Studies in leukemia: the levels of asparagine, glutamine, asparaginase and glutaminase in the mouse following asparaginase administration. Proc. Amer. Ass. Cancer Res. 13, 81 (1972).Google Scholar
  341. Speckman, D., V. Riley, G. A. Santisteban, W. Kirk, and L. Bredberg: The role of stress in producing elevated corticosterone levels and thymus involution in mice. XI Int. Cancer Congr. Abst., p. 382 (1974).Google Scholar
  342. Speckman, D. H., V. Riley, and L. Teschner: Asparaginase therapy in leukemic mice: changes in plasma amino acids as modified by the LDH virus. Abstracts, Tenth Int. Cancer Congr., pp. 443–444 (1970).Google Scholar
  343. Spirin, A. S.: Some problems concerning the macromolecular structure of ribonucleic acids. Progr. Nucl. Acid Res. 1, 301–345 (1963).CrossRefGoogle Scholar
  344. Stansly, P. G.: Non-oncogenic infectious agents associated with experimental tumors. Progr. exp. Tumor Res. 7, 224–258 (1965).PubMedGoogle Scholar
  345. Stansly, P. G., and C. F. Neilson: Relationship between spleen weight increase factor (SWIF) of mice and Eperythrozoon coccoides. Proc. Soc. exp. Biol. (N.Y.) 119, 1059–1063 (1965).Google Scholar
  346. Stark, D. M., and C. G. Crispens: Studies on the multiplication of lactic dehydrogenase-elevating agents. Experientia (Basel) 21, 270 (1965).CrossRefGoogle Scholar
  347. Steeves, R. A., E. A. Mirand, S. Thomson, and L. Avila: Enhancement of spleen focus formation and virus replication in Friend virus infected mice. Cancer Res. 29, 1111–1116 (1969).PubMedGoogle Scholar
  348. Stuart, A. E.: The Reticulo-endothelial System. Edinburgh-London: E & S Livingstone, 1970.Google Scholar
  349. Tennant, R. W.: Taxonomy of murine viruses. Nat. Cancer Inst. Monograph No. 20, 47–53 (1966).Google Scholar
  350. Tennant, R. W., and T. G. Ward: Pneumonia virus of mice (PVM) in cell culture. Proc. Soc. exp. Biol. (N.Y.) 111, 395–398 (1962).Google Scholar
  351. Thompson, W. R.: Use of moving averages and interpolation to estimate median-effective dose. 1. Fundamental formulas, estimation of error, and relation to other methods. Bact. Rev. 11, 115–145 (1947).Google Scholar
  352. Turner, W., P. S. Ebert, R. Bassin, G. Spann, and M. A. Chirigos: Potentiation of murine sarcoma virus (Harvey) (Moloney) oncogenicity in lactic dehydrogenaseelevating virus-infected mice. Proc. Soc. exp. Biol. (N.Y.) 136, 1314–1318 (1970).Google Scholar
  353. Unanue, E. R.: The regulatory role of macrophages in antigenic stimulation. Advanc. Immunol. 15, 95–165 (1972).CrossRefGoogle Scholar
  354. Van Der Helm, H. J., H. A. Zondag, H. A. PH. Hartog, and M. W. Van Der Korn: Lactic dehydrogenase isoenzymes in myocardial infarction. Clin. chim. Acta 7, 540–544 (1962).CrossRefGoogle Scholar
  355. Wachsmuth, E. D., and D. Klingmueller: Immune response to lactate dehydrogenase (LDH) isoenzymes in normal mice and in mice infected with lactic dehydrogenase virus (LDV). J. med. Microbiol. 6, Px-Pxi (1973).Google Scholar
  356. Wacker, W. E. C., and G. A. Scnoenenberger: Peptide inhibitors of lactic dehydrogenase (LDH) I: specific inhibition of LDH-M4 and LDH-H4 by inhibitor peptides I and II. Biochem. biophys. Res. Commun. 22, 291–296 (1966).PubMedCrossRefGoogle Scholar
  357. Wakim, K. G., and G. A. Fleisher: The fate of enzymes in body fluids — an experimental study. II. Disappearance rates of glutamic-oxalacetic transaminase I under various conditions. J. Lab. clin. Med. 61, 86–97 (1963a).Google Scholar
  358. Wakim, K. G., and G. A. Fleisher: The fate of enzymes in body fluids — an experimental study. IV. Relationship of the reticuloendothelial system to activities and disappearance rates of various enzymes. J. Lab. clin. Med. 61, 107–119 (1973b).Google Scholar
  359. Wallis, C., and J. L. Melnick: Thermal inactivation of poliovirus under anaerobic conditions. J. Bact. 84, 389–392 (1962).PubMedGoogle Scholar
  360. Warnock, M. L.: Isozymic patterns in organs of mice infected with LDH agent. Proc. Soc. exp. Biol. (N.Y.) 115, 448–452 (1964).Google Scholar
  361. Wenner, C. E., S. J. Mtltsan, E. A. Mrranu, and J. T. Grace: Serum lactic dehydrogenase levels of mice inoculated with oncogenic and non-oncogenic viruses. Virology 18, 486–487 (1962).PubMedCrossRefGoogle Scholar
  362. Westaway, E. G.: Protein specified by group B togaviruses in mammalian cells during productive infections. Virology 51, 454–465 (1973).PubMedCrossRefGoogle Scholar
  363. Wildy, P.: Classification and nomenclature of viruses. Monographs in Virology 5, 1–81. Basel: S. Karger, 1971.Google Scholar
  364. Wilkinson, J.H.: An Introduction to Diagnostic Enzymology. London: Edward Arnold, 1962.Google Scholar
  365. Wilner, B. I.: A classification of the major groups of human and other animal viruses, 4th Ed. Minneapolis: Burgess Publishing Co., 1969.Google Scholar
  366. Wilson, A. C., N. O. Kaplan, L. Levine, A. Pesce, M. Reichlin, and W. S. Allison: Evolution of lactic dehydrogenase. Fed. Proc. 23, 1258–1266 (1964).PubMedGoogle Scholar
  367. Wolfson, S. K., J. A. Spencer, R. L. Sterkel, and H. G. Williamsashman: Clinical and experimental studies on serum pyridine nucleotide-linked dehydrogenases in liver damages. Ann N Y Acad. Sci. 75, 260–269 (1958).PubMedCrossRefGoogle Scholar
  368. Wrblewsbi, F.: The mechanisms of alteration in lactic dehydrogenase activity of body fluids. Ann. N.Y. Acad. Sci. 75, 322–338 (1958).Google Scholar
  369. Wrblewski, F.: The significance of alterations in lactic dehydrogenase activity in body fluids in the diagnosis of malignant tumors. Cancer 12, 27–39 (1959).CrossRefGoogle Scholar
  370. Wrblewski, F., G. Jervis, and J. S. La Dur;: The diagnostic, prognostic and epidemiologic significance of serum glutamic oxaloacetic transaminase (SGO-T) alterations in acute hepatitis. Ann. intern. Med. 45, 782–800 (1956).Google Scholar
  371. Wrblewski, F., and J. S.La Due: Lactic dehydrogenase activity in blood. Proc. Soc. exp. Biol. (N.Y.) 90, 210–213 (1955).Google Scholar
  372. Wrblewski, F., and J. S. La Due: Serum glutamic pyruvic transaminase (SGP-T) in hepatic disease: a preliminary report. Ann. intern. Med. 45, 801–811 (1956).Google Scholar
  373. Yaffe, D.: The distribution and in vitro propagation of an agent causing high plasma lactic dehydrogenase activity. Cancer Res. 22, 573–580 (1962a).Google Scholar
  374. Yaffe, D.: Studies on an agent associated with high plasma lactic dehydrogenase activity. Acta Un. int. Caner. 19, 407–409 (1962b).Google Scholar
  375. Yamazaki, S, and A. L. Notrins: Inhibition of replication of lactic dehydrogenase virus by actinomycin. J. Virol. 11, 473–478 (1973).PubMedGoogle Scholar
  376. Zebovitz, E., J. K. L. Leong, and S. C. Doughty: Japanese encephalitis virus replication: a procedure for the selective isolation and characterization of viral RNA species. Arch. ges. Virusforsch. 38, 319–327 (1972).PubMedCrossRefGoogle Scholar
  377. Zeigel, R. F., and F. J. Rauscher: Electron microscopic and bioassay studies on a murine leukemia virus (Rauscher): preliminary report. J. nat. Cancer Inst. 30, 207–219 (1963).PubMedGoogle Scholar
  378. Zimmerman, H. J., M. West, and P. Heller: Serum enzymes in disease. II. Lactic dehydrogenase and glutamic oxalacetic transaminase in anemia. Arch. intern. Med. 102, 115–123 (1958).CrossRefGoogle Scholar

Copyright information

© Springer-Verlag/Wien 1975

Authors and Affiliations

  • K. E. K. Rowson
    • 1
  • B. W. J. Mahy
    • 2
  1. 1.Department of Pathology and Bacteriology, The Institute of Laryngology and OtologyUniversity of LondonLondonEngland
  2. 2.Division of Virology, Department of PathologyUniversity of Cambridge, Laboratories Block, Addenbrookes HospitalCambridgeEngland

Personalised recommendations