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EC Number Purification (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59- 23475, 23476, 23481, 23482, 23486, 23487, 23492, 23494, 651502, 651504, 750396
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59147fold, from the fourth larval instar, at day 3 after molt 649498
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59about 429fold 651500
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59affinity chromatography with the ligand 3-[(4'-mercapto)butylthio]-1,1,1-trifluoropropan-2-one 23489
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59expressed wild-type and mutant proteins purified by anion-exchange chromatography. Purification efficiencies of wild-type JHE, mutant F259I, and mutant T314V are 77%, 32%, and 51%, respectively and are purified 4-, 4.4-, and 4.5fold, respectively 707525
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59from pupa, 49fold 649497
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59purified preparation reveals 2 distinct bands: the heavy band does not contain any detectable 1-naphthylacetate activity and is comprised of 3 closely positioned protein bands, the second band exhibits 1-naphthylacetate esterase activity in addition to juvenile hormone esterase activity 23478
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59recombinant enzyme secreted into the cell medium in a baculovirus expression system, affinity chromatography with 8-mercapto-1,1,1-trifluoro-2-octanone 23473
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59recombinant JHE 651510
Display the word mapDisplay the reaction diagram Show all sequences 3.1.1.59recombinant JHE, partial 651511
Results 1 - 10 of 12 > >>