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Expression and characterization of soluble recombinant Ulp1p with glutathione S-transferase tag in Escherichia coli / 生物工程学报
Junhua FU; Qi WANG; Jiechao YIN; Mingyao LIU; Ning LI; Wenbin YAO; Guiping REN; Lu LI; Deshan LI.
Chinese Journal of Biotechnology ; (12): 837-842, 2010.
Article in Chinese | WPRIM | ID: wpr-292200

ABSTRACT

The aim of the study is to obtain an efficient expression of recombinant ubiquitin-like specific protease 1 (Ulp1) by gene engineering. We cloned the Ulp1p, active fragment (403 aa-621 aa) of Ulp1, from Saccharomyces cerevisia, and subcloned into pGEX/Rosetta (DE3) to form an expression plasmid, pGEX-Ulp1p-His6. In order to enhance the solubility of GST-Ulp1p-His6, we purified the fusion protein GST-Ulp1p-His6 by either glutathione S-transferase agarose or Ni-NTA resin chromatography, the purity was up to 98%. We utilized the protein to cleave the SUMO fusions, and the specific activity of GST-Ulp1p-His6 was 1.375 x 10(4) U/mg. This study showed that the recombinant protein GST-Ulp1p-His6 displayed high specificity and activity.


Subject(s)
Cloning, Molecular , Cysteine Endopeptidases , Genetics , Escherichia coli , Genetics , Metabolism , Fungal Proteins , Genetics , Glutathione Transferase , Genetics , Recombinant Fusion Proteins , Genetics , Saccharomyces cerevisiae , Solubility
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