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Title 

Simple purification of Escherichia coli-derived recombinant human interleukin-2 expressed with N-terminus fusion of glucagon

Authors 

Hye Soon WonJee Won LeeIn Ho KimYoung Hoon Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2000

Citation 

Biotechnology and Bioprocess Engineering, vol. 5, no. 1, pp. 13-16

Keywords 

human interleukin-2glucagonN-terminus fusionpurification process

Abstract 

Simple procedures have been devised for purifying recombinant human interleukin-2 (hIL-2), which was expressed in Escherichia coli using sequences of glucagon molecules and enterokinase cleavage site as an N-terminus fusion partner. The insoluble aggregates of recombinant fusion protein produced in E. coli cytoplasm were easily dissolved by simple alkaline pH shift (8→12→8). Following enterokinase cleavage, the recombinant hIL-2 was finally purified by one-step reversed-phase HPLC with high purity. The ease and high efficiency of this simple purification process seem to mainly result from the role of used glucagon fusion partner, which could be applied to the production of other therapeutically important proteins.

ISSN 

1226-8372

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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