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. 1974 Nov;71(11):4429–4434. doi: 10.1073/pnas.71.11.4429

On the Chemical Nature of Transfer Factor

David Dressler 1, Steven Rosenfeld 1
PMCID: PMC433899  PMID: 4530993

Abstract

Two transfer factors prepared in an experimental animal model, the guinea pig, have been tested for their susceptibility to various enzymes of known specificity. The biological activity of these immune response mediators can be destroyed by RNase III, an enzyme that degrades duplex RNA. It, therefore, appears that these transfer factors consist entirely or partly of double-stranded RNA.

Keywords: immune response, leukocyte extract, transfer of immunological information, double-stranded RNA, guinea pig

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Selected References

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

  1. ASKONAS B. A., RHODES J. M. IMMUNOGENICITY OF ANTIGEN-CONTAINING RIBONUCLEIC ACID PREPARATIONS FROM MACROPHAGES. Nature. 1965 Jan 30;205:470–474. doi: 10.1038/205470a0. [DOI] [PubMed] [Google Scholar]
  2. Adler F. L., Fishman M., Dray S. Antibody formation initiated in vitro. 3. Antibody formation and allotypic specificity directed by ribonucleic acid from peritoneal exudate cells. J Immunol. 1966 Oct;97(4):554–558. [PubMed] [Google Scholar]
  3. Bell C., Dray S. Conversion of non-immune spleen cells by ribonucleic acid of lymphoid cells from an immunized rabbit to produce gammaM antibody of foreign light chain allotype. J Immunol. 1969 Dec;103(6):1196–1211. [PubMed] [Google Scholar]
  4. Burger D. R., Vetto R. M., Malley A. Transfer factor from guinea pigs sensitive to dinitrochlorobenzene: absence of superantigen properties. Science. 1972 Mar 31;175(4029):1473–1475. doi: 10.1126/science.175.4029.1473. [DOI] [PubMed] [Google Scholar]
  5. Crouch R. J. Ribonuclease 3 does not degrade deoxyribonucleic acid-ribonucleic acid hybrids. J Biol Chem. 1974 Feb 25;249(4):1314–1316. [PubMed] [Google Scholar]
  6. FISHMAN M., ADLER F. L. Antibody formation initiated in vitro. II. Antibody synthesis in x-irradiated recipients of diffusion chambers containing nucleic acid derived from macrophages incubated with antigen. J Exp Med. 1963 Apr 1;117:595–602. doi: 10.1084/jem.117.4.595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Haruna I., Spiegelman S. Specific template requirments of RNA replicases. Proc Natl Acad Sci U S A. 1965 Aug;54(2):579–587. doi: 10.1073/pnas.54.2.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Horvitz H. R. Polypeptide bound to the host RNA polymerase is specified by T4 control gene 33. Nat New Biol. 1973 Aug 1;244(135):137–140. doi: 10.1038/newbio244137a0. [DOI] [PubMed] [Google Scholar]
  9. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  10. JETER W. S., TREMAINE M. M., SEEBOHM P. M. Passive transfer of delayed hypersensitivity to 2,4-dinitrochlorobenzene in guinea pigs with leucocytic extracts. Proc Soc Exp Biol Med. 1954 Jun;86(2):251–253. doi: 10.3181/00379727-86-21064. [DOI] [PubMed] [Google Scholar]
  11. Kamen R. Characterization of the subunits of Q-beta replicase. Nature. 1970 Nov 7;228(5271):527–533. doi: 10.1038/228527a0. [DOI] [PubMed] [Google Scholar]
  12. Kondo M., Gallerani R., Weissmann C. Subunit structure of Q-beta replicase. Nature. 1970 Nov 7;228(5271):525–527. doi: 10.1038/228525a0. [DOI] [PubMed] [Google Scholar]
  13. LAWRENCE H. S., RAPAPORT F. T., CONVERSE J. M., TILLETT W. S. Transfer of delayed hypersensitivity to skin homografts with leukocyte extracts in man. J Clin Invest. 1960 Jan;39:185–198. doi: 10.1172/JCI104018. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Minkley E. G., Pribnow D. Transcription of the early region of bacteriophage T7: selective initiation with dinucleotides. J Mol Biol. 1973 Jun 25;77(2):255–277. doi: 10.1016/0022-2836(73)90335-5. [DOI] [PubMed] [Google Scholar]
  15. Ptashne M., Gilbert W. Genetic repressors. Sci Am. 1970 Jun;222(6):36–44. doi: 10.1038/scientificamerican0670-36. [DOI] [PubMed] [Google Scholar]
  16. Robertson H. D., Webster R. E., Zinder N. D. Purification and properties of ribonuclease III from Escherichia coli. J Biol Chem. 1968 Jan 10;243(1):82–91. [PubMed] [Google Scholar]
  17. Rosenfeld S., Dressler D. Transfer factor: a subcellular component that transmits information for specific immune responses. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2473–2477. doi: 10.1073/pnas.71.6.2473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Siegel S., Brady A. H., Awad W. M., Jr The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). II. The activity of a serine enzyme in 6 M guanidinium chloride. J Biol Chem. 1972 Jul 10;247(13):4155–4159. [PubMed] [Google Scholar]
  19. Studier F. W. The genetics and physiology of bacteriophage T7. Virology. 1969 Nov;39(3):562–574. doi: 10.1016/0042-6822(69)90104-4. [DOI] [PubMed] [Google Scholar]

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