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Search Purification (Commentary)

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EC Number Purification (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7- 114131, 114132, 114133, 114138, 114139, 114141, 114144, 114145, 114148, 114149, 114150, 114151, 114152, 114153, 114155, 114156, 114164, 114166, 114169, 114170, 114172, 114173, 114174, 114177, 114180, 114183, 114187, 114193, 114194, 114199, 649499, 649636, 649716, 649772, 651469, 651529, 652194, 652432, 663746, 665983, 666537, 666633, 714701
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7ammonium sulfate precipitation and nickel affinity column chromatography. The enzyme is purified 3200fold with a yield of 68% 716835
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7C-terminally truncated form 649248
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7concanavalin A-Sepharose 4B column chromatography and edrophonium-Sepharose 6B column chromatography 713804
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7DEA-cellulose column chromatography, and gel filtration 729685
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7dextran sulfate-Sepharose column chromatography and Ni-NTA column chromatography 715396
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7enzyme by affinity chromatography on a mono-(aminocaproyl)-p-aminophenyltrimethylammonium-containing resin 751215
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7forms I and II 114176
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7from Triton X-100 extract 665263
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.7isozyme AChE1A from strain EG9, 17.5fold from infective juveniles, by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography to homogeneity 679347
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