High level expression of heterologous proteins in methylotrophic yeastPichia pastoris

1988 ◽  
Vol 28 (4) ◽  
pp. 265-278 ◽  
Author(s):  
K. Sreekrishna ◽  
Rica H. B. Potenz ◽  
John A. Cruze ◽  
William R. McCombie ◽  
Kathryn A. Parker ◽  
...  
1992 ◽  
Vol 20 (5) ◽  
pp. 997-1003 ◽  
Author(s):  
M. Needham ◽  
C. Gooding ◽  
K. Hudson ◽  
M. Antoniou ◽  
F. Grosveld ◽  
...  

1998 ◽  
Vol 64 (5) ◽  
pp. 1589-1593 ◽  
Author(s):  
Michael J. Weickert ◽  
Izydor Apostol

ABSTRACT Coexpression of di-α-globin and β-globin in Escherichia coli in the presence of exogenous heme yielded high levels of soluble, functional recombinant human hemoglobin (rHb1.1). High-level expression of rHb1.1 provides a good model for measuring mistranslation in heterologous proteins. rHb1.1 does not contain isoleucine; therefore, any isoleucine present could be attributed to mistranslation, most likely mistranslation of one or more of the 200 codons that differ from an isoleucine codon by 1 bp. Sensitive amino acid analysis of highly purified rHb1.1 typically revealed ≤0.2 mol of isoleucine per mol of hemoglobin. This corresponds to a translation error rate of ≤0.001, which is not different from typical translation error rates found for E. coli proteins. Two different expression systems that resulted in accumulation of globin proteins to levels equivalent to ∼20% of the level of E. colisoluble proteins also resulted in equivalent translational fidelity.


2010 ◽  
Vol 33 (2) ◽  
pp. 327-332
Author(s):  
Xiaoli Zhao ◽  
Wenjing Shen ◽  
Peipei Ben ◽  
Yi Kong ◽  
Hui Cao ◽  
...  

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