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mTOR binding proteins were purified essentially as reported [14].
Then, dengue virus binding proteins were purified by affinity chromatography by passing protein extracts from Ae. aegypti MG through a DENV-2 or rE2-DIII-Sepharose 4B columns.
Once the protein extraction procedure was optimized, dengue virus binding proteins were purified by affinity chromatography by passing protein extracts from C6-36 cells through a rE2-DIII-Sepharose 4B column and eluted with 0.1 M Glycine pH 2.7 containing 0.5 M NaCl.
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In addition to the 28-kDa protein, two distinct 25-kDa GTP-binding proteins were purified from platelets.
Using haem- or PP IX-conjugated beads, haem- or PP IX-binding proteins were purified from rat mitochondrial extract.
A major 70-kDa PP1-binding protein was purified from bovine brain cortex plasma membranes, using affinity chromatography on the immobilized phosphatase inhibitor, microcystin-LR.
This Cd-binding protein was purified from hepatopancreas, kidney, gills, and spleen of carp administered 2 mg/kg Cd (as CdCl2), intraperitoneally for 6 days.
To determine whether these mutations affect Hsp70 binding, the mutant proteins were purified and examined for their ability to interact with Hsp70 in vitro.
DNA-binding domain GST fusion proteins were purified by glutathione affinity on SuperGlu agarose (Generon) in 20 mM Tris pH 7.5, 350 mM NaCl, 0.05% β-mercaptoethanol, containing protease inhibitors (0.2 mM 4- 2-aminoethyl benzenesulphonyl fluoride, 2 μM E64- 2-aminoethyl benzenesulphonylpstatin).
IKKε and TBK1 were fused to MBP (maltose binding protein) and these fusion proteins were purified from insect SF9 cells by baculovirus expression system by Dr Stuart J Decker (Life Sciences Institute, University of Michigan).
GST fusion proteins were purified through binding to Glutathione-Sepharose (GE Healthcare).
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