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Methods for preparation of recombinant cytokine proteins V. mutant analogues of human interferon-gamma with higher stability and activity.

Abstract：

:Mutant analogues of recombinant human immune interferon (IFN-gamma) with higher stability and biological activity were prepared. Depending on the analogue, protein structure modification might involve introduction of an intramonomer disulfide bond (through replacements of Glu7Cys and Ser69Cys), C-terminal shortening by 10 amino acid residues, as well as Gln133Leu substitution in truncated variant. Isolation, purification, and renaturation of the IFN-gamma analogues expressed in Escherichia coli as inclusion bodies were performed according to the scheme developed earlier for wild-type protein. The main idea of this scheme is to remove cellular impurities before recombinant protein renaturation. Folding kinetics of IFN-gamma was studied by reversed-phase HPLC. IFN-gamma and mutant proteins were characterized by their thermal stability and biological activity. Introduction of the intramolecular disulfide bond together with C-terminal shortening and replacement of C-terminal residue was shown to result in increasing the thermal stability by 19 degrees C and four times enhancement of biological activity compared with intact IFN-gamma molecule.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Pechenov SE,Tikhonov RV,Shingarova LN,Korobko VG,Yakimov SA,Klyushnichenko VE,Babajantz AA,Beliaev DL,Kuznetzov VP,Shvetz VI,Wulfson AN

doi

10.1006/prep.2001.1565

keywords:

subject

Has Abstract

pub_date

2002-03-01 00:00:00

pages

173-80

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046592801915657

journal_volume

24

pub_type

杂志文章

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