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Search Purification (Commentary)

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EC Number Purification (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8-
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8by affinity chromatography, using Talon, Co2+, resin and glutathione-Sepharose beads, and by gel filtration
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8chitin column chromatography, Q-Sepharose column chromatography, and Superdex 16/600 gel filtration
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8chitin resin column chromatography, Q Sepharose column chromatography, and Superdex 200 gel filtration
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8EpsE is copurified with the cytoplasmic domain of EpsL to test whether the ATPase activity of EpsE can be modulated by EpsL, complexes are purified using metal affinity chromatography and gel filtration, monomeric EpsE is obtained following thrombin cleavage of a GST-EpsE fusion protein
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8glutathione Sepharose column chromatography and Ni-agarose column chromatography
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8His-tagged EscN is purified from the soluble fraction using nickel-chelating Sepharose, the tag is cleaved with thrombin, cleaved product is purified by Mono-Q anion exchange
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8His-Trap column chromatography and Superdex 75 gel filtration
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8N-terminal cytoplasmic domain, with His-tag
Display the word mapDisplay the reaction diagram Show all sequences 7.4.2.8Ni-NTA column chromatography
Results 1 - 10 of 29 > >>