Purification of human fibroblast interferon by zinc chelate chromatography

The Journal of General Virology
J W HeineP de Somer

Abstract

Human interferon was prepared by superinduction of cultures of either diploid embryonic skin and muscle cells or of the osteosarcoma cell line MG-63. The interferon so obtained was concentrated and partially purified by adsorption to controlled pore glass (CPG) beads at neutral pH and desorption by glycine-HCl buffer at pH 2. After neutralization, this interferon was applied to a column of zinc chelate which was eluted with buffers of decreasing pH. Most of the proteins eluted ahead of the interferon activity, which itself eluted in two distinct peaks. The first peak occurred in the effluent fractions around pH 5.9, and the second one in fractions around pH 5.2. The interferon found in fractions of pH 5.9 contained 5% of the original contaminating proteins. In contrast, the amount of total protein in the pH 5.2 peak was so small that it could not accurately be assayed by the fluorescamine method. Consequently, the interferon in the peak fraction was estimated to have a specific activity of about 2 x 10(9) units/mg. This material was radiolabelled and analysed by electrophoresis. A major peak of about 22000 mol. wt. with only minor contaminating proteins appeared on the autoradiographs. The total recovery of the zinc chelate chr...Continue Reading

Citations

Jan 1, 1981·Archives of Virology·A Billiau
May 1, 1988·Molecular and Cellular Endocrinology·G VerhoevenA Billiau
Sep 11, 2002·Journal of Controlled Release : Official Journal of the Controlled Release Society·Yoshiki SuginoshitaTsutomu Chiba
May 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·J ContentW Fiers
Jan 1, 1983·Microbiology and Immunology·Y Watanabe
Nov 1, 1995·Applied and Environmental Microbiology·R Xiao, W S Kisaalita

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