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pubmed-article:1703216pubmed:abstractTextHuman placental trophoblast interferon (tro-IFN), induced in trophoblast cultures by a superinduction procedure, was purified to a homogeneous product with retention of biological activity. The problems associated with isolation from serum-containing medium were overcome by a combination of Blue Sepharose affinity chromatography and reversed-phase HPLC (RP-HPLC) on Separon SGX C-18. This two-step purification procedure yielded tro-IFN with a specific activity of 3.4 x 10(7) international units/mg of protein. The overall recovery of interferon activity was 66.7%. The purified tro-IFN was shown to be a glycoprotein with an Mr of 24K on native and SDS-PAGE. Its antiviral activity was stable at pH 2.0 at 37 degrees C but was sensitive to heat at 56 degrees C for 1 h and was neutralized by antibodies to human IFN-beta.lld:pubmed
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pubmed-article:1703216pubmed:volume71 ( Pt 12)lld:pubmed
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pubmed-article:1703216pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:1703216pubmed:articleTitlePurification and initial characterization of human placental trophoblast interferon induced by polyriboinosinic.polyribocytidylic acid.lld:pubmed
pubmed-article:1703216pubmed:affiliationDanish Cancer Society, Department of Virus and Cancer, Aarhus, Denmark.lld:pubmed
pubmed-article:1703216pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1703216pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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