Normal immunosuppressive protein. Isolation of a glycoprotein active fraction

Experiments to determine the nature of the active moiety of Normal immunosuppressive protein (Nip) were performed using Sepharose Con A fractionation. Nip was found to be a glycoprotein or a glycopeptide. The fraction eluted by 0.2 M mannose was found to be as active as the crude Nip preparation in...

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Veröffentlicht in:Immunology 1980-03, Vol.39 (3), p.305-309
Hauptverfasser: Goren, R, Nelken, D
Format: Artikel
Sprache:eng
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Zusammenfassung:Experiments to determine the nature of the active moiety of Normal immunosuppressive protein (Nip) were performed using Sepharose Con A fractionation. Nip was found to be a glycoprotein or a glycopeptide. The fraction eluted by 0.2 M mannose was found to be as active as the crude Nip preparation in inhibiting EL4 tumour cell proliferation in vitro. It also gave a positive haemagglutination inhibition test when added to a rabbit anti-Nip antibody system. The resistance of Nip to boiling as well as the positive PAS staining also confirmed the glycoprotein or glycopeptide nature of Nip.
ISSN:0019-2805
1365-2567