Purification and characterization of tagless recombinant human elongation factor 2 kinase (eEF-2K) expressed in Escherichia coli
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منابع مشابه
PURIFICATION AND CHARACTERIZATION OF THE CLONED HUMAN GM-CSF GENE EXPRESSED IN ESCHERICHIA COLI
The human granulocyte-macrophage colony stimulation factor (hGM-CSF) gene was cloned in the pET 23a( +) expression vector under the control of strong bacteriophage T7 transcription and translation signals. The hGM-CSF gene was transferred into E. coli strainBL21 (DE3)pLysS andIPTG was used for induction of GM-CSF gene. Production of the target protein was obtained as revealed by ELISA and ...
متن کاملpurification and characterization of the cloned human gm-csf gene expressed in escherichia coli
the human granulocyte-macrophage colony stimulation factor (hgm-csf) gene was cloned in the pet 23a( +) expression vector under the control of strong bacteriophage t7 transcription and translation signals. the hgm-csf gene was transferred into e. coli strainbl21 (de3)plyss andiptg was used for induction of gm-csf gene. production of the target protein was obtained as revealed by elisa and weste...
متن کاملPurification and refolding of Escherichia coli-expressed recombinant human interleukin-2.
The expression of rhIL-2 (recombinant human interleukin-2) in bacteria results in the formation of insoluble inclusion-body aggregates. These aggregates were first solubilized under denaturing conditions (sodium phosphate buffer solution containing 8 M urea and 10 mM 2-mercaptoethanol) and then purified using IMAC (immobilized metal-ion-affinity chromatography). IMAC was used to capture rhIL-2....
متن کاملPurification and characterization of recombinant Staphylococcus haemolyticus DNA gyrase and topoisomerase IV expressed in Escherichia coli.
The subunits of DNA gyrase and topoisomerase IV from Staphylococcus haemolyticus were expressed in Escherichia coli, purified to homogeneity, and used to reconstitute active enzymes that were sensitive to known topoisomerase inhibitors. This represents the first description of a method for isolating type II topoisomerases of a coagulase-negative staphylococcal species.
متن کاملCloning, expression and purification of recombinant streptokinase: partial characterization of the protein expressed in Escherichia coli.
We cloned the streptokinase (STK) gene of Streptococcus equisimilis in an expression vector of Escherichia coli to overexpress the profibrinolytic protein under the control of a tac promoter. Almost all the recombinant STK was exported to the periplasmic space and recovered after gentle lysozyme digestion of induced cells. The periplasmic fraction was chromatographed on DEAE Sepharose followed ...
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ژورنال
عنوان ژورنال: Protein Expression and Purification
سال: 2011
ISSN: 1046-5928
DOI: 10.1016/j.pep.2011.05.005