期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：8
页码：3139-3142
DOI：10.1073/pnas.71.8.3139
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Human interferon prepared by challenge of leukocytes with Sendai virus, or of fibroblasts with double-stranded poly(inosinic acid){middle dot}poly(cytidylic acid), has been studied with respect to purification by affinity chromatography. Both leukocyte and fibroblast interferons are removed from crude tissue culture fluids by means of columns of antibody to leukocyte interferon attached to Sepharose-4B. The antibody was prepared in sheep using, as antigen, material that had been partially purified by gel filtration through Sephadex G-100 columns. Many of the impurities in the crude fibroblast interferon were presumably not recognized by the sheep antibodies induced by leukocyte interferon. Fibroblast interferon was, therefore, much more effectively purified as the result of this "common denominator" approach. The fibroblast product, in contrast to interferon from leukocytes, could only be harvested efficiently from the crude starting material when a carrier protein (bovine-serum albumin, and later, cytochrome c) was added to the eluting buffers to counteract losses, presumably due to adsorption on purification and assay equipment. Both varieties of interferon exhibit molecular weights of approximately 20,000-25,000, although association with higher molecular weight proteins occurs.
