[Purification and characterization of recombinant human interleukin 11 which expressed by Pichia pastoris].
This study first time report a method to purify the rhIL-11 which expressed by Pichia pastoris. rhIL-11 was secreted into the supernatant and collected by centrifugation. The purity of rhIL-11 reached 97% through the steps of ultrafiltration, SP Sepharose FF, Phenyl Sepharose HP and Sephadex G25. Analysis of SDS-PAGE, Western-blotting, IEF, RP-HPLC, Mass spectrometer, N and C terminus amino acid sequence and bioactivity was conducted. All the analysis results proved that the rhIL-11 expressed by Pichia pastoris was the same as Neumeg which was expressed in E. coli with fusion expression system. So it is possibly a cheaper and easier method to produce rhIL-11 for clinical use.
Huang
Y S
YS
School of Medicine, Zhejiang University, Hangzhou 310005, China.
Dong
Y
Y
Li
H
H
Wang
T Y
TY
Qiu
J W
JW
Yu
Y N
YN
D005285:Fermentation; D006801:Humans; D017370:Interleukin-11 / Q000302:isolation & purification* / Q000494:pharmacology; D010843:Pichia / Q000235:genetics*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000494:pharmacology
D017370:Interleukin-11; D011994:Recombinant Proteins