Expression and aggregation of recombinant human consensus interferon-alpha mutant by Pichia pastoris.
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).
Hao
Yuyou
Y
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, PR China.
Chu
Ju
J
Wang
Yonghong
Y
Zhang
Siliang
S
Zhuang
Yingping
Y
D000998:Antiviral Agents / Q000302:isolation & purification / Q000494:pharmacology; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D005285:Fermentation; D007370:Interferon Type I / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology; D016898:Interferon-alpha; D010843:Pichia / Q000235:genetics / Q000502:physiology*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology
D000998:Antiviral Agents; D007370:Interferon Type I; D016898:Interferon-alpha; D011994:Recombinant Proteins; C050739:interferon alfacon-1