Abstract
A recombinant human consensus interferon-alpha mutant (cIFN) was expressed in Pichia pastoris. The maximum dry cell weight, cIFN concentration and antiviral activity were 160 g l(-1), 1.24 g l(-1) and 4.1 x 10(7) IU ml(-1), respec tively. The cIFN secreted into the medium was in the form of aggregates dominantly by non-covalent interaction and partially by disulphide bond. When the fermentation supernatant was disaggregated with 6 M guanidine hydrochloride, the antiviral activity of cIFN achieved 2.2 x 10(8) IU ml(-1).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antiviral Agents / isolation & purification
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Antiviral Agents / pharmacology
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Electrophoresis, Gel, Two-Dimensional / methods
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Fermentation
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Interferon Type I / biosynthesis*
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Interferon Type I / isolation & purification
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Interferon Type I / pharmacology
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Interferon-alpha
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Pichia / genetics
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Pichia / physiology*
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Recombinant Proteins / biosynthesis*
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / pharmacology
Substances
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Antiviral Agents
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Interferon Type I
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Interferon-alpha
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Recombinant Proteins
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interferon alfacon-1