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Arakawa T, Hsu YR, Chang D, et al. Structure and activity of glycosylated human interferon-gamma. J Interferon Res. 1986;6(6):687-95doi: 10.1089/jir.1986.6.687.
Arakawa, T., Hsu, Y. R., Chang, D., Stebbing, N., & Altrock, B. (1986). Structure and activity of glycosylated human interferon-gamma. Journal of interferon research, 6(6), 687-95. https://doi.org/10.1089/jir.1986.6.687
Arakawa, T, et al. "Structure and activity of glycosylated human interferon-gamma." Journal of interferon research vol. 6,6 (1986): 687-95. doi: https://doi.org/10.1089/jir.1986.6.687
Arakawa T, Hsu YR, Chang D, Stebbing N, Altrock B. Structure and activity of glycosylated human interferon-gamma. J Interferon Res. 1986 Dec;6(6):687-95. doi: 10.1089/jir.1986.6.687. PMID: 3106525.
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J Interferon Res. 1986 Dec;6(6):687-95. doi: 10.1089/jir.1986.6.687.

Structure and activity of glycosylated human interferon-gamma.

Journal of interferon research

T Arakawa, Y R Hsu, D Chang, N Stebbing, B Altrock

PMID: 3106525 DOI: 10.1089/jir.1986.6.687

Abstract

Structural properties and activity of recombinant human interferon-gamma (IFN-gamma) purified from Chinese hamster ovary (CHO) cells or a natural source were determined and compared with those of Escherichia coli-derived IFN-gamma. One preparation of CHO-derived IFN-gamma showed three bands, with the middle band being a doublet, in a SDS-polyacrylamide gel. The two higher-molecular-weight bands were shown to be glycosylated. Western blot analysis indicated that the three bands are IFN-gamma and lack an intact carboxyl terminus. The circular dichroic (CD) spectra showed that conformation of the CHO-derived IFN-gamma is similar in the native state, in acid, and after renaturation from acid to the E. coli-derived IFN-gamma. These results indicate that neither glycosylation nor carboxy-terminal processing affects conformational properties of the protein, as detected by CD spectroscopy. However, the antiviral activity was fourfold lower for the preparation of CHO-derived IFN-gamma than for the E. coli-derived IFN-gamma. A different preparation or a natural IFN-gamma preparation with less extensive carboxy-terminal processing showed similar conformational properties and antiviral activity to the E. coli-derived IFN-gamma. These results indicate that the carboxyl terminus, but not glycosylation, plays an important role in the antiviral activity of IFN-gamma.

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