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pubmed-article:15269532pubmed:abstractTextRecombinant porcine mature interleukin-18 (rPomIL-18) has been purified from the haemolymph of silkworms. After co-infection of two recombinant baculoviruses (BmAcpVL1392-IL-18-His and BmAcpVL1392-casp-1) into the silkworm, rPomIL-18 was produced and secreted into the haemolymph. Polyethylene glycol (PEG) 6000 was added to the haemolymph at 8% (v/w) to precipitate storage proteins which would otherwise bind non-specifically to the metal chelating column and the supernatant then was applied to Sepharose bonded with Ni2+. rPomIL-18 was eluted from the column using 100 mM imidazole buffer at pH 8 with a purity of 93.6%. Approximately 5.3 mg purified rPomIL-18 was obtained from 22 ml haemolymph. It could induce interferon-gamma formation from porcine peripheral blood mononuclear cells.lld:pubmed
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pubmed-article:15269532pubmed:authorpubmed-author:MoriYasuyukiYlld:pubmed
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pubmed-article:15269532pubmed:authorpubmed-author:NagayaHidekaz...lld:pubmed
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pubmed-article:15269532pubmed:authorpubmed-author:MatsumotoSaya...lld:pubmed
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pubmed-article:15269532pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15269532pubmed:articleTitleMethod for purifying porcine mature interleukin-18 from silkworm haemolymph.lld:pubmed
pubmed-article:15269532pubmed:affiliationKatakura Industries Co., Ltd., 1548 Shimo-okutomi, Sayama, Saitama 350-1332, Japan. h.nagaya@katakura.co.jplld:pubmed
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