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x * 55000 + x * 22000, SDS-PAGE
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x * 40475 + x * 20517, calculated from sequence
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x * 41000 + x * 22000, SDS-PAGE
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x * 37000 + x * 50000, SDS-PAGE
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x * 43000-44000 + x * 24000, wild-type and mutant enzyme, SDS-PAGE
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x * 41500, heavy subunit of isoform GGT5, SDS-PAGE
?
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x * 54000 + x * 21000, SDS-PAGE
dimer
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1 * 43000 + 1 * 30000, SDS-PAGE
dimer
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1 * 38000 + 1 * 23000, only the large subunit is active when the enzyme is dissociated under denaturing conditions. The behavior of the native enzyme suggests that the active site of the large subunit is masked by the small subunit, SDS-PAGE
dimer
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1 * 38000 + 1 * 23000, only the large subunit is active when the enzyme is dissociated under denaturing conditions. The behavior of the native enzyme suggests that the active site of the large subunit is masked by the small subunit, SDS-PAGE
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dimer
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1 * 42000 + 1 * 22000, SDS-PAGE
dimer
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1 * 42000 + 1 * 22000, SDS-PAGE
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dimer
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1 * 45000 + 1 * 22000, SDS-PAGE
dimer
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1 * 45000 + 1 * 21000, SDS-PAGE
dimer
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1 * 32000 + 1 * 43000, SDS-PAGE
dimer
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1 * 45000 + 1 * 21000, SDS-PAGE
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dimer
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1 * 32000 + 1 * 43000, SDS-PAGE
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dimer
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1 * 68000 + 1 * 27000, SDS-PAGE
dimer
-
1 * 57000 + 1 * 25500, SDS-PAGE
dimer
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1 * 55000 + 1 * 25000, SDS-PAGE
dimer
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1 * 71000 + 1 * 28000, SDS-PAGE
dimer
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1 * 39200 + 1 * 22000, isoform A, SDS-PAGE
dimer
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1 * 38600 + 1 * 22000, isoform B, SDS-PAGE
dimer
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1 * 41000 + 1 * 21000, SDS-PAGE
dimer
-
1 * 41000 + 1 * 21000, SDS-PAGE
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dimer
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1 * 61000 + 1 * 27000, SDS-PAGE
dimer
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1 * 53000 + 1 * 20000, papain-solubilized, SDS-PAGE
dimer
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1 * 150000 + 1 * 95000, SDS-PAGE
dimer
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1 * 57000 + 1 * 21000, SDS-PAGE, presence of urea, 2-mercaptoethanol
dimer
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1 * 47000 + 1 * 22000, SDS-PAGE
dimer
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1 * 62000 + 1 * 22000, SDS-PAGE
dimer
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1 * 62000 + 1 * 20000, SDS-PAGE
dimer
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1 * 64000 + 1 * 29000, SDS-PAGE
dimer
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1 * 38000 + 1 * 14000, SDS-PAGE
dimer
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1 * 65000 + 1 * 27000, SDS-PAGE, 8 M urea-PAGE
dimer
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1 * 66000 + 1 * 55000, SDS-PAGE
dimer
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1 * 66000 + 1 * 55000, SDS-PAGE
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dimer
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1 * 47000 + 1 * 28000, SDS-PAGE
dimer
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1 * 42000 + 1 * 21000, enzyme form GGT I, SDS-PAGE
dimer
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1 * 42000 + 1 * 21000, enzyme form GGT II, SDS-PAGE
dimer
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1 * 51000 + 1 * 22000, Triton X-100 solubilized, SDS-PAGE
dimer
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1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
dimer
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1 * 45000 + 1 * 23000, SDS-PAGE
dimer
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1 * 50000 + 1 * 22000, kidney, SDS-PAGE
dimer
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1 * 46000 + 1 * 22000, papain solubilized, SDS-PAGE
dimer
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1 * 43000 + 1 * 25000, SDS-PAGE
dimer
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1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
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dimer
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1 * 43000 + 1 * 25000, SDS-PAGE
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dimer
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1 * 64000 + 1 * 23000, SDS/2-mercaptoethanol-PAGE
dimer
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1 * 64000 + 1 * 23000, SDS/2-mercaptoethanol-PAGE
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heterodimer
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probably has heterodimer structure with the larger subunit of 38900 Da
heterodimer
1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE
heterodimer
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1 * 46000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
heterodimer
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1 * 46000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
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heterodimer
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1 * 45700 + 1 * 19700, recombinant extracellular C-terminally His6-tagged enzyme, SDS-PAGE
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heterodimer
1 * 45000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
heterodimer
Q62WE3
in the crystal structure of BlGGT, the large subunit contains a globular domain consisting of 14 alpha-helices, six small 310 helices and 11 beta-strands, and the small subunit comprises of 3 alpha-helices, two small 310 helices and 11 beta-strands. Furthermore, both subunits provide strands to a nearly flat beta-sheet that constitutes the core of the heterodimeric arrangement. Unlike their structural consistency, the primary structure of GGT enzymes displays a great degree of variability
heterodimer
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in the crystal structure of BlGGT, the large subunit contains a globular domain consisting of 14 alpha-helices, six small 310 helices and 11 beta-strands, and the small subunit comprises of 3 alpha-helices, two small 310 helices and 11 beta-strands. Furthermore, both subunits provide strands to a nearly flat beta-sheet that constitutes the core of the heterodimeric arrangement. Unlike their structural consistency, the primary structure of GGT enzymes displays a great degree of variability
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heterodimer
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1 * 45000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
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heterodimer
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1 * 45000, large subunit, + 1 * 22000, small subunit, His6-tagged enzyme, SDS-PAGE
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heterodimer
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1 * 45000 + 1 * 22000, SDS-PAGE
heterodimer
1 * 40000 + 1 * 20000, SDS-PAGE
heterodimer
one heavy subunit and one light subunit, the active site of GGT that catalyzes the transfer of gamma-glutamyl group, is located in the light subunit
heterodimer
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1 * 40000 + 1 * 20000, SDS-PAGE
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heterodimer
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one heavy subunit and one light subunit, the active site of GGT that catalyzes the transfer of gamma-glutamyl group, is located in the light subunit
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heterodimer
bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
heterodimer
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bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
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heterodimer
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bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
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heterodimer
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bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
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heterodimer
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bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
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heterodimer
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bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit
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heterodimer
1 * 64000 + 1 * 22000, isoform GGT1, SDS-PAGE
heterodimer
1 * 64000 + 1 * 22000, SDS-PAGE
heterodimer
1 * 64000 + 1 * 25000, isoform GGT5, SDS-PAGE
heterodimer
1 * 17000 + 1 * 30000, SDS-PAGE
heterodimer
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1 * 17000 + 1 * 30000, SDS-PAGE
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heterodimer
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1 * 64000 + 1 * 26000, SDS-PAGE
monomer
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1 * 61000, enzyme form GGT A, SDS-PAGE
monomer
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1 * 61000, enzyme form GGT B, SDS-PAGE
monomer
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1 * 43000, isoforms I and II, SDS-PAGE
monomer or heterodimer
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two active enzyme forms of 30000 Da and 67000 Da
monomer or heterodimer
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two active enzyme forms of 30000 Da and 67000 Da
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tetramer
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2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer
tetramer
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2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer
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tetramer
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2 * 20000 + 2 * 40000, SDS-PAGE
additional information
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the active site resides on the small subunit
additional information
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protease solubilization leads to a reduced MW of the larger subunit
additional information
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small subunit MW: 20000
additional information
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the active site resides on the small subunit
additional information
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the active site resides on the small subunit
additional information
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the active site resides on the small subunit
additional information
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the enzyme is composed of two non-identical catalytically active subunits
additional information
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the active site resides on the small subunit
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additional information
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the enzyme is composed of two non-identical catalytically active subunits
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