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In this paper, the purification of the human recombinant protein expressed in E. coli using the GST Gene Fusion System, by applying various methods of bacterial lysis: sonication, freeze/thaw and beadbeating, is presented. The study was an attempt to compare the properties of the proteins obtained by the sonication method, recommended by manufacturers but inaccessible for many researchers, with those obtained using two other readily available lysis methods. The data show that all purifieddoi:10.2298/jsc0507943m fatcat:3zipmh7hqrckni43iwlx66q2l4