Human leukocyte interferon: production, purification to homogeneity, and initial characterization.
Author(s) -
Menachem Rubinstein,
Sara Rubinstein,
P C Familletti,
Robert S. Miller,
Alan A. Waldman,
Sidney Pestka
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.76.2.640
Subject(s) - chromatography , chemistry , homogeneous , sodium dodecyl sulfate , homogeneity (statistics) , polyacrylamide gel electrophoresis , gel electrophoresis , electrophoresis , interferon , gel permeation chromatography , biochemistry , biology , enzyme , organic chemistry , immunology , polymer , statistics , physics , mathematics , thermodynamics
A method of fractionating proteins by high-performance liquid partition chromatography has been developed and used for isolation and purification to homogeneity of one of the species of human leukocyte interferon. The homogeneous interferon exhibited a sharp peak on high-performance liquid chromatography and a single narrow band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Extraction of the gel gave a single sharp peak of antiviral activity coinciding with the protein band. The specific activity of pure interferon was found to be 2--4 X 10(8) units/mg, based on amino acid analysis. The molecular weight is 17,500--18,000.
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