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heterodimer
-
alphabeta, 1*39000, 1*19000
multimer
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composed of several 60-70 kDa-subunits, SDS-PAGE
?
x * 52000, SDS-PAGE and calculated
?
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x * 52000, SDS-PAGE and calculated
-
?
x * 60000, SDS-PAGE, recombinant mutated beta-glucosidase
?
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x * 120000-142000, SDS-PAGE
?
x * 93000, SDS-PAGE, recombinant protein
?
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x * 120000, SDS-PAGE
-
?
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x * 57130, calculated, x * 57000, SDS-PAGE
?
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x * 57130, calculated, x * 57000, SDS-PAGE
-
?
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x * 65000 + x * 55000, SDS-PAGE
?
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x * 63000-64000, native enzyme, SDS-PAGE, x * 66000-69000, recombinant dalcochinase with N-terminal truncation and polyhistidine tag, SDS-PAGE
?
-
x * 52000, SDS-PAGE
-
?
Littorina kurila
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x * 200000, SDS-PAGE
?
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x * 78240, calculated, x * 75000, SDS-PAGE
?
x * 60000, recombinant His-tagged enzyme, SDS-PAGE
?
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x * 75900, calculated
-
?
x * 66000, tagged recombinant enzyme, SDS-PAGE, x * 50000, detagged recombinant enzyme, SDS-PAGE
?
x * 54000, CelG, SDS-PAGE
?
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x * 98000, SDS-PAGE, both isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
?
x * 116000, SDS-PAGE, wild-type BGL
?
x * 133000, SDS-PAGE, recombinant BGL
?
x * 53000, recombinant His-tagged isozyme BGL1A, SDS-PAGE
?
x * 60000, recombinant His-tagged isozyme BGL1B, SDS-PAGE
?
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x * 60000, recombinant His-tagged isozyme BGL1B, SDS-PAGE
-
?
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x * 53000, recombinant His-tagged isozyme BGL1A, SDS-PAGE
-
?
x * 91457, deduced from nucleotide sequence
?
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x * 64000, isoform A, x * 47000, isoform B, SDS-PAGE
?
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x * 56691, calculated from sequence
?
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x * 140000, SDS-PAGE
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?
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x * 77800, SDS-PAGE
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?
x * 90000, SDS-PAGE, x * 79819, calculated
?
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x * 90000, SDS-PAGE, x * 79819, calculated
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?
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x * 50000, SDS-PAGE
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?
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x * 81000, SDS-PAGE
-
?
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x * 58000-60000, SDS-PAGE
?
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x * 71000, SDS-PAGE, recombinant protein
?
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x * 60000, recombinant enzyme, SDS-PAGE
?
x * 49951, calculated from amino acid sequence
?
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x * 50000, SDS-PAGE
-
?
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x * 49951, calculated from amino acid sequence
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dimer
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1 * 80000 + 1 * 60000, SDS-PAGE
dimer
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1 * 90000 plus 1 * 45000, SDS-PAGE
dimer
-
2 * 120000, SDS-PAGE
dimer
-
2 * 91400, deduced from nucleotide sequence
dimer
-
2 * 118000, SDS-PAGE
dimer
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2 * 118000, SDS-PAGE
-
dimer
-
2 * 27000, SDS-PAGE
dimer
2 * 58000, SDS-PAGE
dimer
-
2 * 80000, SDS-PAGE
dimer
-
2 * 110000, SDS-PAGE
dimer
2 * 79466, calculated from sequence
dimer
-
2 * 79466, calculated from sequence
-
dimer
-
2 * 110000, SDS-PAGE
dimer
-
2 * 94000, SDS-PAGE
dimer
-
1 * 42000 + 1 * 26000, SDS-PAGE
dimer
-
2 * 71000, SDS-PAGE, for PGII
dimer
-
2 * 28000, SDS-PAGE
dimer
2 * 60680, deduced from nucleotide sequence
dimer
2 * 85000, SDS-PAGE, difference to deduced molecular weight is due to glycosylation
dimer
2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F
dimer
crystallization data
dimer
2 * 130000, recombinant enzyme, SDS-PAGE
dimer
gel filtration and crystallization data
dimer
-
2 * 130000, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 102000, SDS-PAGE
dimer
-
2 * 83000, recombinant enzyme
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 96500, SDS-PAGE
dimer
-
2 * 85000, SDS-PAGE
dimer
-
2 * 120000, SDS-PAGE, isoform I
dimer
-
2 * 105000, SDS-PAGE
dimer
-
2 * 101000, SDS-PAGE
dimer
-
2 * 105000, SDS-PAGE
-
dimer
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2 * 110000, SDS-PAGE
dimer
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2 * 82000, SDS-PAGE
dimer
native-PAGE shows Bgl1A in the form of a monomer and dimer
dimer
2 * 52900, calculated
heterotrimer
1 * 165200, plus 1 * 87900, plus 1 * 56800, SDS-PAGE
heterotrimer
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1 * 165200, plus 1 * 87900, plus 1 * 56800, SDS-PAGE
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hexamer
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active form
hexamer
6 * 64085.41, recombinant His-tagged TaGlu1b, SDS-PAGE, gel filtration, and mass spectrometry
hexamer
6 * 64141.25, recombinant His-tagged isozyme TaGlu1a, SDS-PAGE, gel filtration, and mass spectrometry
hexamer
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
homodimer
2 * 54000, SDS-PAGE
homodimer
-
2 * 39100, SDS-PAGE
homodimer
-
2 * 39100, SDS-PAGE
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homodimer
2 * 57000, SDS-PAGE
homodimer
beta-glucosidase TpBGL1 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
homodimer
beta-glucosidase TpBGL3 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
homodimer
-
beta-glucosidase TpBGL3 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
-
homodimer
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beta-glucosidase TpBGL1 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
-
homodimer
crystal structure
homotetramer
-
4 * 116000, SDS-PAGE
homotetramer
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4 * 116000, SDS-PAGE
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homotetramer
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4 * 80000, SDS-PAGE
monomer
-
1 * 128000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 77000, piceid-beta-D-glucosidase, SDS-PAGE
monomer
-
1 * 77000, piceid-beta-D-glucosidase, SDS-PAGE
-
monomer
-
1 * 90000-107000, SDS-PAGE, 4 isoforms
monomer
-
1 * 47000-48000, SDS-PAGE, native gradient PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 52000, SDS-PAGE
monomer
-
1 * 52000, SDS-PAGE
-
monomer
-
1 * 64200, SDS-PAGE
monomer
-
1 * 65000, SDS-PAGE
monomer
-
1 * 90000, SDS-PAGE
monomer
-
1 * 110000, SDS-PAGE
monomer
-
1* 75000, SDS-PAGE
monomer
-
1 * 53000, SDS-PAGE
monomer
-
1 * 51900, SDS-PAGE
monomer
-
1 * 53000, SDS-PAGE, recombinant CBG
monomer
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
monomer
1 * 120000, SDS-PAGE
monomer
1 * 127000, calculated from sequence
monomer
1 * 78276, calculated from sequence
monomer
1 * 80000, calculated from sequence
monomer
1 * 96873, calculated from sequence
monomer
1 * 97117, calculated from sequence
monomer
1 * 54100, calulated, 1 * 59000, SDS-PAGE of recombinant His-tagged protein
monomer
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1 * 54100, calulated, 1 * 59000, SDS-PAGE of recombinant His-tagged protein
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monomer
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1 * 78276, calculated from sequence
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monomer
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1 * 80000, calculated from sequence
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monomer
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1 * 120000, SDS-PAGE
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monomer
-
1 * 97117, calculated from sequence
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monomer
-
1 * 127000, calculated from sequence
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monomer
-
1 * 96873, calculated from sequence
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monomer
Melanocarpus sp.
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1 * 92000, SDS-PAGE
monomer
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1 * 92000, SDS-PAGE
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monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
-
monomer
-
1 * 43000, SDS-PAGE
monomer
1 * 52000, isozyme BglB, SDS-PAGE
monomer
1 * 50000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 50000, recombinant enzyme, SDS-PAGE
-
monomer
1 * 53000, recombinant isozyme BGL1A, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
-
monomer
-
1 * 60600, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 68000, SDS-PAGE
monomer
-
1 * 135000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
-
monomer
1 * 50000, mutant enzyme R170A/R220A/Y227F/R459G, SDS-PAGE
monomer
1 * 71000, mutant enzyme R170A/R220A/Y227F/R448E, SDS-PAGE
monomer
1 * 96000, mutant enzyme R170A/R220A/Y227F/R449R, SDS-PAGE
monomer
-
1 * 50000-58000, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 82000, SDS-PAGE
monomer
-
1 * 100000, SDS-PAGE
monomer
-
1 * 100000, SDS-PAGE
-
monomer
-
1 * 78000, SDS-PAGE
monomer
-
1 * 52600, SDS-PAGE
monomer
1 * 110000, SDS-PAGE
monomer
-
1 * 110000, SDS-PAGE
-
monomer
-
1 * 89000, SDS-PAGE
monomer
-
1 * 85000, SDS-PAGE
monomer
1 * 120000, His-tagged recombinant enzyme, SDS-PAGE
monomer
-
1 * 120000, His-tagged recombinant enzyme, SDS-PAGE
-
monomer
Thermochaetoides thermophila
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1 * 43000, SDS-PAGE
monomer
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1 * 85000, SDS-PAGE
monomer
-
1 * 116000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
-
monomer
thermophilic anaerobic bacterium
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1 * 43000-50000, SDS-PAGE
monomer
-
1 * 48642, deduced from amino acid composition, SDS-PAGE
monomer
-
1 * 167000, SDS-PAGE
monomer
-
1 * 167000, SDS-PAGE
-
monomer
-
1 * 81600, SDS-PAGE
monomer
native-PAGE shows Bgl1A in the form of a monomer and dimer
monomer
-
1 * 62400, SDS-PAGE
octamer
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composed of 8 identical subunits, ability of each octamer to link with each other to form long polymeric assemblies, crystal structure analysis
octamer
composed of 8 identical subunits, (alpha/beta)-8-barrel-structural fold, crystal structure analysis
octamer
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composed of 8 identical subunits, (alpha/beta)-8-barrel-structural fold, crystal structure analysis
oligomer
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three protein bands in SDS-PAGE
oligomer
-
x * 49000, SDS-PAGE
oligomer
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x * 130000, calculated, x * 130000, SDS-PAGE, and x * 230000, SDS-PAGE of enzyme purified in presence of Ca2+ or enzyme in crude extract
oligomer
-
x * 115000, isoform beta-glucosidase 1, x * 94000 plus x * 21000, isoform beta-glucosidase 2, x * 94000 plus x * 21000, isoform beta-glucosidase 3, x * 52000, isoform beta-glucosidase 4, x * 49000 plus x * 46000, isoform beta-glucosidase 5, x * 77000, isoform beta-glucosidase 6, SDS-PAGE
oligomer
-
x * 115000, isoform beta-glucosidase 1, x * 94000 plus x * 21000, isoform beta-glucosidase 2, x * 94000 plus x * 21000, isoform beta-glucosidase 3, x * 52000, isoform beta-glucosidase 4, x * 49000 plus x * 46000, isoform beta-glucosidase 5, x * 77000, isoform beta-glucosidase 6, SDS-PAGE
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tetramer
-
4 * 95000, SDS-PAGE
tetramer
-
4 * 80000, SDS-PAGE
tetramer
-
4 * 79000, SDS-PAGE
tetramer
-
4 * 90000, SDS-PAGE
tetramer
-
4 * 70000, SDS-PAGE
tetramer
-
4 * 70000, SDS-PAGE
-
tetramer
-
4 * 61100, SDS-PAGE, for PGI
tetramer
-
4 * 115000, SDS-PAGE
tetramer
-
4 * 110000, gel filtration
tetramer
composed of 4 identical subunits, X-ray diffraction study
tetramer
wild-type enzyme
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 90000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
-
tetramer
4 * 97000, recombinant enzyme, SDS-PAGE
tetramer
-
4 * 97000, recombinant enzyme, SDS-PAGE
-
tetramer
-
4 * 90000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
trimer
-
3 * 110000, SDS-PAGE
trimer
-
3 * 102000, SDS-PAGE
trimer
-
3 * 102000, SDS-PAGE
-
trimer
-
3 * 102000, SDS-PAGE
-
trimer
3 * 93400, SDS-PAGE
trimer
3 * 93418, calculated from sequence
trimer
-
3 * 93400, SDS-PAGE
-
trimer
-
3 * 93418, calculated from sequence
-
trimer
-
SDS-PAGE, 3 * 70000
trimer
-
3 * 120000, SDS-PAGE
trimer
-
3 * 120000, SDS-PAGE
-
trimer
-
3 * 120000, SDS-PAGE
-
additional information
-
quarternary structure analysis, structure and kinetics of multimers of different size, overview
additional information
the main-chain fold of the enzyme belongs to the (beta/alpha)8 barrel structure, the active site is located at the bottom of a pocket formed by large surface loops, surrounding the C termini of the barrel of beta-strands
additional information
-
the main-chain fold of the enzyme belongs to the (beta/alpha)8 barrel structure, the active site is located at the bottom of a pocket formed by large surface loops, surrounding the C termini of the barrel of beta-strands
additional information
oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity, BglB aglycon site structure, overview
additional information
-
oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity, BglB aglycon site structure, overview
additional information
determination and analysis of the subsite -1, i.e. glycone site, of isozyme BGL1A, overview, the loop region covering on the (beta/alpha)8 barrel is significantly deviated forming a unique subsite +1, i.e. aglycone site, of BGL1A
additional information
-
determination and analysis of the subsite -1, i.e. glycone site, of isozyme BGL1A, overview, the loop region covering on the (beta/alpha)8 barrel is significantly deviated forming a unique subsite +1, i.e. aglycone site, of BGL1A
additional information
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
additional information
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
additional information
-
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
additional information
-
enzyme exists in a 130000 Da and in a 230000 Da form. Kinetic data for some substrates are different for the two forms, while no difference is observed in optimum pH and temperature
additional information
secondary structure prediction and homology molecular modeling
additional information
-
secondary structure prediction and homology molecular modeling
additional information
-
secondary structure prediction and homology molecular modeling
-
additional information
three-dimensional structure modeling
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
-
capillary LCESI/MS peptide sequence determination and protein identification
additional information
enzyme specifically interacts with chimeric lectin beta-glucosidase aggregating factor resulting in high molecular weight complexes
additional information
-
enzyme specifically interacts with chimeric lectin beta-glucosidase aggregating factor resulting in high molecular weight complexes