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. 1967 Oct;1(5):883–890. doi: 10.1128/jvi.1.5.883-890.1967

Characterization of Virus- and Endotoxin-induced Interferons Obtained from the Serum and Urine of Rabbits

Yang H Ke 1, Monto Ho 1
PMCID: PMC375365  PMID: 5621484

Abstract

Interferons induced in the rabbit by Newcastle disease virus or by endotoxin have been further characterized as to their physicochemical stability and molecular size by Sephadex G-100 gel filtration. Endotoxin-induced interferon obtained from serum was more labile than virus-induced interferon. Both endotoxin and virus induced interferons obtained from serum contained two peaks: a minor high molecular weight (>100,000) peak and a major lower molecular weight peak. The molecular weight of the major peak induced by endotoxin was 54,000, and that induced by Newcastle disease virus was 46,000. The gel filtration pattern of interferon recovered from the urine of animals inoculated with virus reflected faithfully the pattern found in serum except that there was proportionately less of the high molecular weight peak. However, the urine interferon from endotoxin-inoculated animals contained only one broad peak with a molecular weight of 35,000. This was not the peak fraction present in the serum of such animals. It is postulated that this may represent the basic unit of endotoxin-induced interferon, and that the serum components are either polymers or conjugates of this basic unit.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. EAGLE H. Amino acid metabolism in mammalian cell cultures. Science. 1959 Aug 21;130(3373):432–437. doi: 10.1126/science.130.3373.432. [DOI] [PubMed] [Google Scholar]
  3. HO M., BREINIG M. K. Conditions for the production of an interferon appearing in chick cell cultures infected with Sindbis virus. J Immunol. 1962 Aug;89:177–186. [PubMed] [Google Scholar]
  4. HO M. INTERFERON-LIKE VIRAL INHIBITOR IN RABBITS AFTER INTRAVENOUS ADMINISTRATION OF ENDOTOXIN. Science. 1964 Dec 11;146(3650):1472–1474. doi: 10.1126/science.146.3650.1472. [DOI] [PubMed] [Google Scholar]
  5. HO M., KONO Y. EFFECT OF ACTINOMYCIN D ON VIRUS AND ENDOTOXIN-INDUCED INTERFERONLIKE INHIBITORS IN RABBITS. Proc Natl Acad Sci U S A. 1965 Jan;53:220–224. doi: 10.1073/pnas.53.1.220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hallum J. V., Youngner J. S., Stinebring W. R. Interferon activity associated with high molecular weight proteins in the circulation of mice injected with endotoxin or bacteria. Virology. 1965 Nov;27(3):429–431. doi: 10.1016/0042-6822(65)90124-8. [DOI] [PubMed] [Google Scholar]
  7. Ho M., Postic B. Renal excretion of interferon. Nature. 1967 Jun 17;214(5094):1230–1231. doi: 10.1038/2141230a0. [DOI] [PubMed] [Google Scholar]
  8. KONO Y., HO M. THE ROLE OF THE RETICULOENDOTHELIAL SYSTEM IN INTERFERON FORMATION IN THE RABBIT. Virology. 1965 Jan;25:163–166. doi: 10.1016/0042-6822(65)90268-0. [DOI] [PubMed] [Google Scholar]
  9. Ke Y. H., Ho M., Merigan T. C. Heterogeneity of rabbit serum interferons. Nature. 1966 Jul 30;211(5048):541–542. doi: 10.1038/211541a0. [DOI] [PubMed] [Google Scholar]
  10. Ke Y. H., Singer S. H., Postic B., Ho M. Effect of puromycin on virus and endotoxin-induced interferonlike inhibitors in rabbits. Proc Soc Exp Biol Med. 1966 Jan;121(1):181–183. doi: 10.3181/00379727-121-30731. [DOI] [PubMed] [Google Scholar]
  11. LINDENMANN J., GIFFORD G. E. Studies on vaccinia virus plaque formation and its inhibition by interferon. III. A simplified plaque inhibition assay of interferon. Virology. 1963 Mar;19:302–309. doi: 10.1016/0042-6822(63)90068-0. [DOI] [PubMed] [Google Scholar]
  12. Postic B., DeAngelis C., Breinig M. K., Ho M. Effects of cortisol and adrenalectomy on induction of interferon by endotoxin. Proc Soc Exp Biol Med. 1967 May;125(1):89–92. doi: 10.3181/00379727-125-32021. [DOI] [PubMed] [Google Scholar]
  13. Postic B., DeAngelis C., Breinig M. K., Monto H. O. Effect of temperature on the induction of interferons by endotoxin and virus. J Bacteriol. 1966 Mar;91(3):1277–1281. doi: 10.1128/jb.91.3.1277-1281.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Smith T. J., Wagner R. R. Rabbit macrophage interferons. II. Some physicochemical properties and estimations of molecular weights. J Exp Med. 1967 Apr 1;125(4):579–593. doi: 10.1084/jem.125.4.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Taylor J. Inhibition of interferon action by actinomycin. Biochem Biophys Res Commun. 1964;14:447–451. doi: 10.1016/0006-291x(64)90084-1. [DOI] [PubMed] [Google Scholar]
  16. Youngner J. S., Stinebring W. R., Taube S. E. Influence of inhibitors of protein synthesis on interferon formation in mice. Virology. 1965 Dec;27(4):541–550. doi: 10.1016/0042-6822(65)90179-0. [DOI] [PubMed] [Google Scholar]

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