Purification and partial characterization of human lymphoblast interferon. | Zendy

Kathryn C. Zoon | Zendy; Mark E. Smith | Zendy; Pamela J. Bridgen | Zendy; Dorothy Zur Nedden | Zendy; Christian B. Anfinsen | Zendy

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Purification 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

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.

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