Open AccessPurification and partial characterization of human lymphoblast interferon.
Author(s) -
Kathryn C. Zoon,
Mark E. Smith,
Pamela J. Bridgen,
Dorothy Zur Nedden,
Christian B. Anfinsen
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.11.5601
Subject(s) - lymphoblast , interferon , sodium dodecyl sulfate , gel electrophoresis , polyacrylamide gel electrophoresis , amino acid , chemistry , microbiology and biotechnology , electrophoresis , biochemistry , newcastle disease , biology , virus , virology , cell culture , enzyme , genetics
One component of human lymphoblastoid interferon obtained from Namalwa cultures induced by Newcastle disease virus has been purified to a specific activity of 2.5 x 10(8) interferon units per mg of protein (protein content based on amino acid analysis). A single polypeptide species with an apparent molecular weight of 18,500 comigrating with the antiviral activity was observed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Preliminary amino-terminal sequencing results support the conclusion that the interferon species is essentially homogeneous.