z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom