Abstract
Genes encoding truncated versions of bovine and chicken gamma interferon genes lacking predicted protease cleavage sites at the C-terminus were constructed and expressed in the yeast Pichia Pastoris. The recombinant proteins possessed increased stability in comparison with the corresponding wild-type gamma interferons while retaining biological activity. The recombinant strains provide a useful tool for the purification of bovine and chicken gamma interferons for their use in veterinary applications.
Publication types
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English Abstract
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cattle
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Cell Line
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Chickens / immunology
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Fibroblasts / drug effects
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Fibroblasts / pathology
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Fibroblasts / virology
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Gene Expression
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Interferon-gamma / genetics*
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Interferon-gamma / immunology
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Interferon-gamma / pharmacology
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Molecular Sequence Data
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Pichia / genetics*
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Pichia / metabolism
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Plasmids / chemistry*
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Plasmids / metabolism
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Protein Engineering / methods*
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Protein Stability
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Protein Structure, Tertiary
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Proteolysis
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
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Recombinant Proteins / pharmacology
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Vesiculovirus / physiology
Substances
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Recombinant Proteins
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Interferon-gamma