METHODS OF PREPARATION OF RECOMBINANT CYT OKINE PROTEINS .2. AN EFFICIENT METHOD FOR ISOLATION, PURIFICATION, AND RENATURATION OF HUMAN RECOMBINANT GAMMA-INTERFERON

Authors
WULFSON AN TIKHONOV RV PECHENOV SE KLYUSHNICHENKO VE MIROSHNIKOV AI
Citation
An. Wulfson et al., METHODS OF PREPARATION OF RECOMBINANT CYT OKINE PROTEINS .2. AN EFFICIENT METHOD FOR ISOLATION, PURIFICATION, AND RENATURATION OF HUMAN RECOMBINANT GAMMA-INTERFERON, Bioorganiceskaa himia, 23(9), 1997, pp. 721-726
Citations number
12
Journal title
Bioorganiceskaa himia → ACNP
ISSN journal
01323423
Volume
23
Issue
9
Year of publication
1997
Pages
721 - 726
Database
ISI
SICI code
0132-3423(1997)23:9<721:MOPORC>2.0.ZU;2-K
Abstract
An efficient method for the isolation, purification, and renaturation of human recombinant gamma-interferon from biomass of transformed E. c oil cells was developed. It involves the extraction of the protein fro m the inclusion bodies, preliminary purification of the protein, and t hree stages of ion-exchange chromatography with an intermediate renatu ration between the second and the third stages. A highly active (2 x 1 0(7) U/mg) recombinant protein of up to 99% purity (according to SDS-P AGE and HPLC) was obtained with a 30% overall yield.