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Normal immunosuppressive protein purification and quantitative estimation experiments.

Abstract
An improved method for the preparation and purification of normal immunosuppressive protein (NIP) is described. The purified material has a molecular weight between 10,000 and 25,000. Its biological and serological activity is approximately 10--20 times higher than that of the crude fraction. An antibody to normal immunosuppressive protein prepared in rabbits made the quantitative estimation of NIP by a haemaggluination inhibition test possible. Similarly, a very sensitive assay for the quantitative determination of NIP by its inhibitory effect on the proliferation of EL-4 tumor cells is also described. Eluates prepared from polyacrylamide gels were active in inhibiting EL-4 tumor cell proliferation and neutralized the anti-NIP activity in the haemagglutination inhibition test.
AuthorsD Nelken, R Goren, H Ovadia, N Hanna
JournalJournal of immunological methods (J Immunol Methods) Vol. 28 Issue 3-4 Pg. 267-76 ( 1979) ISSN: 0022-1759 [Print] Netherlands
PMID479607 (Publication Type: Journal Article)
Chemical References
  • Blood Proteins
  • Immune Sera
  • Immunosuppressive Agents
Topics
  • Animals
  • Blood Proteins (immunology, isolation & purification)
  • Electrophoresis, Polyacrylamide Gel
  • Hemagglutination Inhibition Tests
  • Humans
  • Immune Sera (pharmacology)
  • Immunosuppressive Agents (immunology, isolation & purification)
  • Molecular Weight
  • Neoplasms, Experimental (immunology)
  • Rabbits

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