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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1987-5-26
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0197-8357
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
687-95
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3106525-Animals,
pubmed-meshheading:3106525-Cell Transformation, Viral,
pubmed-meshheading:3106525-Circular Dichroism,
pubmed-meshheading:3106525-Cricetinae,
pubmed-meshheading:3106525-Cricetulus,
pubmed-meshheading:3106525-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3106525-Escherichia coli,
pubmed-meshheading:3106525-Female,
pubmed-meshheading:3106525-Humans,
pubmed-meshheading:3106525-Interferon-gamma,
pubmed-meshheading:3106525-Molecular Weight,
pubmed-meshheading:3106525-Ovary,
pubmed-meshheading:3106525-Protein Conformation,
pubmed-meshheading:3106525-Recombinant Proteins,
pubmed-meshheading:3106525-Structure-Activity Relationship
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pubmed:year |
1986
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pubmed:articleTitle |
Structure and activity of glycosylated human interferon-gamma.
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pubmed:publicationType |
Journal Article,
Comparative Study
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