Interferon-induced proteins. Purification and characterization of a 15,000-dalton protein from human and bovine cells induced by interferon

• Published in: The Journal of biological chemistry Vol. 259; no. 23; pp. 14835 - 14839
• Main Authors: Korant, B D, Blomstrom, D C, Jonak, G J, Knight, E
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 10-12-1984; American Society for Biochemistry and Molecular Biology
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Burkitt Lymphoma; Cattle; Cell Line; Dactinomycin - pharmacology; Fibroblasts - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Interferon Type I - pharmacology; Interferon Type I - physiology; Kidney; Miscellaneous; Molecular Weight; Protein Biosynthesis; Proteins; Proteins - genetics; RNA, Messenger - genetics; Species Specificity; Human; Cell culture; Purification; In vitro translation; Radiolabelling; Activation; Biosynthesis; Proteins; Vertebrata; Reversed phase chromatography; Mammalia; Interferon; Artiodactyla; Beef; Ungulata
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)42679-2

Human interferons induce a protein of 15,000 daltons in human and bovine cells. This protein is located in the cytoplasm in a soluble form and is induced by concentrations of interferon which induce the antiviral state. Messenger RNA prepared from interferon-treated human and bovine cells contains a mRNA which yields on translation in vitro a protein similar in size to the 15-kDa protein induced by interferon in vivo. The human protein has been purified to homogeneity from interferon-treated human cells by ion-exchange chromatography and reverse-phase high-performance liquid chromatography. A comparison of the peptides generated by V8 protease from the human and bovine 15-kDa proteins reveals that the two proteins are similar but not identical.