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x * 79000, calculated, x * 75000, SDS-PAGE
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x * 81000, calculated, x * 75000, SDS-PAGE
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x * 119544, calculated from amino acid sequence
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Bacteroides polypragmatus
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57000 and 103000, 2 protein bands detected, SDS-PAGE
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x * 114300, calculated from sequence
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x * 114300, calculated from sequence
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?
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x * 70000, SDS-PAGE, x * 78000, calculated
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x * 70000, SDS-PAGE, x * 78000, calculated
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x * 78060, calculated from sequence
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x * 78060, calculated from sequence
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?
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x * 100000, SDS-PAGE
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?
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x * 53000, SDS-PAGE
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?
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x * 75200, wild-type, x * 88220, mutant FMNP01Gal-2, calculated
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x * 75200, wild-type, x * 88220, mutant FMNP01Gal-2, calculated
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x * 97000, isozyme OsGal1, SDS-PAGE
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x * 75000, SDS-PAGE, recombinant BGalP-cMyc-His fusion protein
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x * 118088, sequence calculation
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x * 100860, isoform BGAL9, calculated from amino acid sequence
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x * 80200, isoform BGAL17, calculated from amino acid sequence
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x * 82420, isoform BGAL6, calculated from amino acid sequence
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x * 90470, isoform BGAL16, calculated from amino acid sequence
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x * 92090, isoform BGAL15, calculated from amino acid sequence
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x * 92190, isoform BGAL12, calculated from amino acid sequence
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x * 92580, isoform BGAL1, calculated from amino acid sequence
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x * 92720, isoform BGAL8, calculated from amino acid sequence
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x * 93110, isoform BGAL2, calculated from amino acid sequence
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x * 93620, isoform BGAL5, calculated from amino acid sequence
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x * 94330, isoform BGAL7, calculated from amino acid sequence
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x * 94350, isoform BGAL4, calculated from amino acid sequence
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x * 94500, isoform BGAL10, calculated from amino acid sequence
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x * 94570, isoform BGAL3, calculated from amino acid sequence
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x * 95640, isoform BGAL11, calculated from amino acid sequence
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x * 95870, isoform BGAL13, calculated from amino acid sequence
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x * 95890, isoform BGAL14, calculated from amino acid sequence
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x * 118000, SDS-PAGE
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?
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x * 50000, enzyme from corpus region, SDS-PAGE
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x * 84000, and a second enzyme form of MW 97000 Da, SDS-PAGE
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x * 97000, and a second enzyme form of MW 84000 Da, SDS-PAGE
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x * 85000, enzyme from caput and cauda, SDS-PAGE
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x * 62000, enzyme from round spermatids, SDS-PAGE
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x * 64000, enzyme from spermatocytes, SDS-PAGE
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x * 56561, calculated from sequence
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x * 56650, calculated from sequence
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x * 56764, calculated from sequence
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x * 56561, calculated from sequence
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?
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x * 56561, calculated from sequence
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?
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x * 56600, SDS-PAGE
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?
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x * 56650, calculated from sequence
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?
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x * 56764, calculated from sequence
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?
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x * 56000, SDS-PAGE
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?
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x * 129501, calculated from sequence
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x * 59000, SDS-PAGE
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?
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x * 72741, calculation from nucleotide sequence
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x * 72741, calculation from nucleotide sequence
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dimer
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1 * 48000 + 1 * 36000, beta-galactosidase I, SDS-PAGE
dimer
Corynebacterium murisepticum
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2 * 100000, SDS-PAGE
dimer
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2 * 50000, SDS-PAGE
dimer
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2 * 62000, SDS-PAGE of reduced enzyme
dimer
2 * 78000, SDS-PAGE
dimer
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2 * 78000, SDS-PAGE
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dimer
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1 * 90000 + 1 * 12000
dimer
2 * 123000, SDS-PAGE
dimer
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2 * 123000, SDS-PAGE
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dimer
1 * 35000 + 1 * 72000, SDS-PAGE
dimer
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1 * 35000 + 1 * 72000, SDS-PAGE
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dimer
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2 * 110000, wild-type enzyme and mutant enzymes L317D and P429S, SDS-PAGE
dimer
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1 * 35000 + 1 * 72000, strain L103, SDS-PAGE
dimer
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1 * 35000 + 1 * 72000, strain L461, SDS-PAGE
dimer
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1 * 35000 + 1 * 72000, strain L103, SDS-PAGE
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dimer
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1 * 35000 + 1 * 72000, strain L461, SDS-PAGE
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dimer
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1 * 35000 + 1 * 72000, strain L103, SDS-PAGE
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dimer
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1 * 35000 + 1 * 72000, strain L461, SDS-PAGE
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dimer
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1 * 47000 + 1 * 40000, SDS-PAGE
dimer
-
2 * 100000, SDS-PAGE
dimer
-
2 * 100000, SDS-PAGE
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dimer
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2 * 11000-140000
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dimer
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2 * 60000, SDS-PAGE
dimer
-
1 * 30000 + 1 * 45000, SDS-PAGE
dimer
2 * 75000, SDS-PAGE
dimer
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2 * 120000, SDS-PAGE
dimer
-
2 * 120000, SDS-PAGE
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dimer
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2 * 120000, SDS-PAGE
dimer
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2 * 86000, SDS-PAGE
dimer
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2 * 86000, SDS-PAGE
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dimer
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2 * 30000, SDS-PAGE
dimer
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x * 75000-80000, SDS-PAGE
dimer
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2 * 58000, SDS-PAGE
dimer
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1 * 38000 + 1 * 48000, beta-galactosidase I, II and III, SDS-PAGE
heterodimer
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heterodimer
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1 * 72000 + 1 * 35000, SDS-PAGE
heterodimer
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1 * 72180 + 1 * 35223, calculated from amino acid sequence
hexamer
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hexamer
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6 * 90000, SDS-PAGE
hexamer
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6 * 90000, SDS-PAGE
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homotetramer
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4 * 113695, calculated from amino acid sequence
homotetramer
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4 * 116000, native and SDS-PAGE
homotetramer
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4 * 113695, calculated from amino acid sequence
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homotetramer
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4 * 116000, native and SDS-PAGE
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homotetramer
x-ray crystallography
homotetramer
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4 * 000, SDS-PAGE
homotetramer
4 * 110000, SDS-PAGE
homotetramer
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4 * 118000
homotrimer
3 * 70000, SDS-PAGE
homotrimer
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3 * 79711, calculated from amino acid sequence
homotrimer
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3 * 80000, SDS-PAGE
monomer
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1 * 120000-125000, SDS-PAGE
monomer
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1 * 110000, SDS-PAGE
monomer
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1 * 120000, SDS-PAGE
monomer
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1 * 110000, SDS-PAGE
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monomer
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1 * 120000, SDS-PAGE
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monomer
1 * 129000, glycosylated enzyme, SDS-PAGE
monomer
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1 * 120000, SDS-PAGE
monomer
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1 * 68000, SDS-PAGE
monomer
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1 * 51000, denaturing PAGE
monomer
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1 * 62000, SDS-PAGE
monomer
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1 * 62000, SDS-PAGE
monomer
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1 * 71000, SDS-PAGE
monomer
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1 * 94000, SDS-PAGE
monomer
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1 * 130000, SDS-PAGE
monomer
1* 120000 SDS-PAGE
monomer
1 * 118000, calculated, 1 * 120000, SDS-PAGE
monomer
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1* 120000 SDS-PAGE
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monomer
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1 * 118000, calculated, 1 * 120000, SDS-PAGE
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monomer
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1 * 145000, SDS-PAGE
monomer
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1 * 145000, SDS-PAGE
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monomer
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1 * 95000, SDS-PAGE
monomer
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2 * 264000, full-length enzyme, estimated from SDS-PAGE
monomer
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2 * 264000, full-length enzyme, estimated from SDS-PAGE
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monomer
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1 * 50000, SDS-PAGE
monomer
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1 * 50000, SDS-PAGE
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tetramer
4 * 112000
tetramer
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three-dimensional structure modeling of BgaS, homotetramer that forms a diamond shape with two axes: a long interface and an activating interface, overview
tetramer
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three-dimensional structure modeling of BgaS, homotetramer that forms a diamond shape with two axes: a long interface and an activating interface, overview
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tetramer
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4 * 89000, SDS-PAGE
tetramer
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4 * 115000, SDS-PAGE
tetramer
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4 * 115000, SDS-PAGE
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tetramer
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4 * 118000, equilibrium sedimentation in 8 M urea
tetramer
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4 * 118000, equilibrium sedimentation in 8 M urea
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tetramer
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4 * 118000, equilibrium sedimentation in 8 M urea
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tetramer
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4 * 65000, SDS-PAGE
tetramer
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4 * 78000, SDS-PAGE
tetramer
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4 * 11000-140000
tetramer
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4 * 11000-140000
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tetramer
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4 * 66000, SDS-PAGE
tetramer
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4 * 66000, SDS-PAGE
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tetramer
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4 * 60000, SDS-PAGE
tetramer
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4 * 60000, SDS-PAGE
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tetramer
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4 * 135000, low speed sedimentation without reaching equilibrium in urea hydrochloride
additional information
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tertiary structure of the recombinant hybrid enzyme, protein structure homology-modelling, overview
additional information
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a major band of 32000 Da and a minor band of 18000 Da and 13000 Da
additional information
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other oligomer forms of the enzyme are inactive
additional information
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electrophoretic mobility and catalytic activity of individual molecules of enzyme are reproducible for each molecule but different for individual molecules. The observed ranges in electrophoretic motility are similar for different experimental protocols. There is no relationship between the observed activities and electrophoretic motilities
additional information
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secondary structure by circular dichroism, the enzyme is a beta-type protein, having 22% beta-turns, 14% parallel beta-sheet, 25% antiparallel beta-sheet,34% unordered structure, and only 5% alpha-helix, structure-function relationship, highest secondary structure content at pH 6.5-7.0, overview
additional information
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tertiary structure of the beta-galactosidase of Kluyveromyces lactis and the recombinant hybrid enzyme, protein structure homology-modelling, overview
additional information
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beta-lactoglobulin interacts with beta-galactosidase and increases the catalytic activity due to interaction of both proteins probably through the lysine epsilon-amino groups of beta-lactoglobulin
additional information
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tertiary structure of the beta-galactosidase of Kluyveromyces lactis and the recombinant hybrid enzyme, protein structure homology-modelling, overview
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additional information
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other oligomer forms of the enzyme are inactive
additional information
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peptide mass fingerprinting
additional information
peptide mass fingerprinting
additional information
peptide mass fingerprinting
additional information
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other oligomer forms of the enzyme are inactive
additional information
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other oligomer forms of the enzyme are inactive
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additional information
three-dimensional structure analysis and molecular modeling, overview
additional information
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three-dimensional structure analysis and molecular modeling, overview
additional information
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enzyme amino acid composition, overview
additional information
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enzyme amino acid composition, overview
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