Presence of a polynucleotide binding site on murine immune interferon (T-type)

• Published in: Biochemical and biophysical research communications Vol. 85; no. 1; pp. 480 - 489
• Main Authors: Wietzerbin, J., Stefanos, S., Lucero, M., Falcoff, E., Thang, D.C., Thang, M.N.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 14.11.1978
• Subjects: Animals; Binding Sites; Interferons - metabolism; Lectins; Mice; Mice, Nude; Polynucleotides - metabolism; Protein Binding; Spleen - immunology; poly I; PHA; poly C; poly U
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(78)80067-9

The T-type interferon induced by PHA has been shown to be quantitatively bound to poly I-sepharose. The binding is not impaired by the presence of 50% ethylene glycol. The interferon-Poly I complex could be only dissociated at high ionic strength. The homogenous elution profile suggests that almost the whole population of PHA-interferon molecules have the polynucleotide binding site. Conparison of crude and ammonium sulfate fractionated preparations shows that the elution of the interferon activity of the latter from poly I-sepharose column was shifted to a lower ionic strength. This suggests that the protein molecules might be modified by chemical or enzymatic action affecting the polynucleotide binding site. The presence of a polynucleotide binding site on immune interferon (Type T) is thus one of a few common properties to viral induced interferon. Furthermore, taking advantage of this property, a practical purification method could be set up.