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• W2010197112 abstract "Specific binding sites for human interferon-γ (hIFN-γ) were found on particulates prepared from the hemolymph and protocerebrum of fifth-instar larvae of the tobacco hornworm, Manduca sexta. A portion of these sites could be solubilized in an active form by the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate (CHAPS). A well-defined specific binding was also associated with hemolymph particulate residue after solubilization by CHAPS. About one-half of [125I]hIFN-γ binding could be displaced by heparin. The bound hIFN-γ could be covalently cross-linked to the binding sites using disuccinylamide suberate, and the molecular weight range of these complexes was 200–800 kDa as determined by density gradient sedimentation and gel-exclusion chromatography. Only a small fraction of the hemolymph IFN-γ binding could be competed by another mammalian cytokine, rat prolactin (rPRL), while there was no sensitivity to rat growth hormone. The small specific rPRL binding found in Manduca hemolymph showed an affinity similar to the prolactin sites found in the liver of pregnant rats. The detergent-insoluble Manduca hIFN-γ binding was bimodal and similar in affinity distribution to the binding found with human platelet membranes (Kdiss range 0.1–2 nM). The detergent-solubilized IFN-γ sites were homogenous, with a Kdiss of about 1.5 nM. The IFN-γ binding sites in Manduca tissues may therefore include molecular species similar to the known invertebrate cytokine receptors and proteoglycan co-receptors." @default.
• W2010197112 created "2016-06-24" @default.
• W2010197112 creator A5003519144 @default.
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• W2010197112 date "1999-02-01" @default.
• W2010197112 modified "2023-09-26" @default.
• W2010197112 title "Specific binding of human interferon-γ to particulates from hemolymph and protocerebrum of tobacco hornworm (Manduca sexta) larvae" @default.
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• W2010197112 doi "https://doi.org/10.1016/s0305-0491(98)10155-4" @default.
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