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Results 1 - 10 of 12 > >>
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2? x * 30000, SDS-PAGE 656643
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2? x * 62000, SDS-PAGE 681650
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2? x * 64000, SDS-PAGE of enzymes from placenta and adipose tissue 681104
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2? x * 65000, SDS-PAGE 656641, 681644
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2dimer coprecipitation of mutant enzyme with FLAG-tagged enzyme 665843
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2heterotetramer alpha2,beta2, 2 * 57000 + 2 * 38000, two 57 kDa catalytic and two 38 kDa regulatory subunits, SDS-PAGE 656637
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2hexamer - 135595, 135598
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2hexamer 6 * 74000, placenta, SDS-PAGE 135595
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2monomer 1 * 78000, solubilized in Triton X-100 135604
Display the word mapDisplay the reaction diagram Show all sequences 3.1.6.2More all oligomeric states between a monomer and a tetramer are possible, varying aggregation properties of enzyme under various buffer, pH, detergent and ionic strength conditions, gel filtration suggests ES to be predominantly a homotetramer, native PAGE analysis of solubilized single crystals of ES shows all possible oligomeric states between a monomer and a tetramer, but predominantly the monomeric and dimeric states 656641
Results 1 - 10 of 12 > >>