Purification and properties of the α-interferon receptor of human lymphoblastoid (Namalva) cells

A. Traub, S. Feinstein, M. Gez, A. Lazar, A. Mizrahi

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


The interferon receptor was solubilized from human lymphoblastoid (Namalva) cell membranes with Triton X-100. It was purified by chromatography on wheat-germ lectin-Sepharose and hydroxyapatite and by affinity chromatography on interferon-hexanoyl-Sepharose. The partially purified receptor was analyzed by gel filtration on Sepharose 6B and by sucrose gradient sedimentation in the presence of 0.1% Triton X-100. Gel filtration analysis yielded a Stokes radius of 74 Å for the receptor-Triton X-100 complex. Sedimentation in sucrose gradients revealed an heterogeneous pattern of distribution with a plateau of activity between 4 and 10 S. Removal of suspected lipid material and Triton X-100 by extraction with isoamyl alcohol resulted in an accelerated rate of receptor sedimentation in a sodium dodecyl sulfate-containing sucrose gradient. Under these conditions it manifested an apparent sedimentation coefficient of 13.6 S. The dissociation constants K(d) derived from Scatchard analysis of binding data with the purified receptor were in the range of 0.2-0.5 nM.

Original languageEnglish
Pages (from-to)13872-13877
Number of pages6
JournalJournal of Biological Chemistry
Issue number22
StatePublished - 1984


Dive into the research topics of 'Purification and properties of the α-interferon receptor of human lymphoblastoid (Namalva) cells'. Together they form a unique fingerprint.

Cite this