Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
113000
-
gel filtration, native PAGE, isoenzyme AK Late
115000
-
aspartokinase II, equilibrium sedimentation
116000
-
equilibrium ultracentrifugation
122000
-
2 * 122000, ultracentrifugation in TES or HEPES buffer
122400
-
alpha2, beta2, calculated from nucleotide sequence
124400
-
alpha2, beta2, calculated from nucleotide sequence
125000
-
aspartokinase II
127000
-
aspartokinase III, sedimentation equilibrium
133000
-
sedimentation velocity centrifugation
140000
gel filtration, homodimer
150000
-
sucrose density gradient centrifugation, peak 2
154000
dynamic light-scattering, crystallization
166000
-
in presence of KCl and L-lysine at 11°C, sedimentation equilibrium
167000
-
first AK isoenzyme, gel filtration
169000
-
aspartokinase II, equilibrium sedimentation
17700
aspartate kinase beta, calculated from amino acid sequence
180000 - 200000
-
aspartokinase devoid of homoserine dehydrogenase activity in presence of threonine, gel filtration
181000
-
in presence of KCl and L-lysine at 25°C, sedimentation equilibrium
18145
-
1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
18500
-
beta subunit, calculated from nucleotide sequence
200000
-
isoenzyme II, gel filtration
20200
AKbeta analytical ultracentrifugation, absence of threonine
21700
aspartate kinase beta, gel filtration
230000
-
sucrose density gradient centrifugation, peak 3
240000
-
calculated from Stokes' radius
246000
-
gel filtration, Superose 6
253000
-
gel filtration, non-denaturing electrophoresis, 4-20% polyacrylamide gradient gels
258000
-
gel filtration, Superose 12
297000
-
glutathione-S-transferase fusion protein, in the presence of threonine, blue native gel electrophoresis
298000
-
wild type, in the presence of threonine, gel filtration
320000
gel filtration, in presence of 5.0 mM L-threonine
330000
-
isoenzyme I, gel filtration
33300
AKbeta gel-filtration chromatography, addition of threonine induces dimerization
334000
-
native complex, Svedberg equation
33800
AKbeta in presence with 5 mM L-threonine, gel filtration
358000
-
light scattering studies
36000
AKbeta analytical ultracentrifugation, presence of threonine
360000
-
equilibrium sedimentation
40000
-
6 * 40000, SDS-PAGE
42000
-
SDS-PAGE, recombinant protein
43200
-
alpha subunit, calculated from nucleotide sequence
43700
-
alpha subunit, calculated from nucleotide sequence
44000
-
SDS-PAGE, recombinant protein
44108
-
1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
44300
-
calculated from cDNA
45000
-
1 * 18000 + 1 * 45000, Western blot immunoanalysis
48000
-
4 * 48000, SDS-PAGE
49000
-
2 * 49000 + 2 * 60000, SDS-PAGE
52400
-
calculated from cDNA
53000
-
1 * 17000 + 1 * 53000, urea treatment, SDS-PAGE
58100
-
wild type, calculated from protein sequence
58700
-
wild type, SDS-PAGE
61200
-
alphabeta, calculated from nucleotide sequence
62200
-
alphabeta, calculated from nucleotide sequence
66000
-
4 * 66000, ultracentrifugation
79000
-
second AK isoenzyme, gel filtration
80000
-
4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex
83000
dynamic light-scattering, addition of increasing levels of guanidine-HCl up to 2000 mM causes a decrease in the AK particle size, dissociation into dimers
84000
-
4 * 84000, SDS-PAGE
87500
-
4 * 87500, SDS-PAGE
88000
-
4 * 88000, gel filtration in 6.0 mM guanidinium chloride
90300
-
alpha2, beta2, gel filtration
93000
? * 93000, SDS-PAGE
100000
-
gel filtration
100000
-
sucrose density gradient centrifugation, peak 1
110000
-
-
121400
-
alpha2, beta2, calculated from nucleotide sequence
121400
-
alpha2, beta2, calculated from nucleotide sequence
17000
-
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE
17000
-
1 * 17000 + 1 * 43000, SDS-PAGE
17000
-
1 * 17000 + 1 * 53000, urea treatment, SDS-PAGE
17000
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE
17000
-
2 * 17000 + 2 * 47000, SDS-PAGE
17720
full-length beta subunit (Met1Ala161) with a His6-tag extension at the C-terminal end, calculated
17720
beta subunit (Met1-Ala161), calculated from nucleotide sequence
18000
-
18000
-
beta subunit, calculated from nucleotide sequence
18000
-
SDS-PAGE, recombinant protein, beta-subunit (amino acids 248-255)
18000
-
1 * 18000 + 1 * 45000, Western blot immunoanalysis
18000
-
alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
23000
AKbeta, gel filtration
23000
AKbeta gel-filtration chromatography, absence of additives, somewhat larger than the mass of a monomer, addition of lysine causes no change
280000
-
gel filtration
280000
-
glutathione-S-transferase fusion protein, in the presence of threonine, gel filtration
344000
-
glutathione-S-transferase fusion protein, gel filtration
344000
-
threonine insensitive mutant, with and without threonine in the buffer, blue native gel electrophoresis
345000
-
threonine insensitive mutant, with and without threonine in the buffer, gel filtration
345000
-
wild type, blue native gel electrophoresis, gel filtration
346000
-
wild type, gel filtration
346000
-
aspartokinase-homoserine dehydrogenase complex, sedimentation equilibrium
346000
-
glutathione-S-transferase fusion protein, blue native gel electrophoresis
42700
-
alpha subunit, calculated from nucleotide sequence
42700
-
alpha subunit, calculated from nucleotide sequence
43000
-
3 * 43000, SDS-PAGE
43000
-
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE
43000
-
1 * 17000 + 1 * 43000, SDS-PAGE
43000
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE
43000
-
4 * 43000, aspartokinase II, equilibrium sedimentation
43900
-
alpha subunit, calculated from nucleotide sequence
43900
-
alpha subunit, calculated from nucleotide sequence
450000
gel filtration
450000
about, recombinant enzyme, gel filtration
47000
-
47000
-
2 * 17000 + 2 * 47000, SDS-PAGE
470000
gel filtration
50000
-
SDS-PAGE, recombinant protein
50000
-
recombinant protein, expressed in E. coli, gel filtration
53200
gel filtration
53200
monofunctional AK2, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
55100
gel filtration
55100
monofunctional AK3, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
55900
gel filtration
55900
monofunctional AK1, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
58000
-
wild type, gel filtration
58000
dynamic light-scattering, addition up to 4000 mM guanidine-HCl leads to dissociation of the AK dimers into monomers
60000
-
2 * 49000 + 2 * 60000, SDS-PAGE
60000
-
? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride
60700
-
alphabeta, calculated from nucleotide sequence
60700
-
alphabeta, calculated from nucleotide sequence
64200
-
alpha2, gel filtration
64200
-
alpha2, gel filtration
87800
-
alpha2, calculated from nucleotide sequence
87800
-
alpha2, calculated from nucleotide sequence