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EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Reference
30000
-
1 * 30000, enzyme also exists as dimer and tetramer, SDS-PAGE; 2 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE; 4 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE
35000
-
12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE; 1 * 35000, enzyme also exists as tetramer, octamer, dodecamer and polymer, SDS-PAGE; 4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE; 8 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE; x * 35000, between 670000 Da and 2000000 Da, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
35000
-
4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
61268
-
x * 61268, deduced from amino acid sequence
62000
-
1 * 74000 + 1 * 62000, SDS-PAGE
62258
-
x * 62258, deduced from amino acid sequence
64000
-
x * 64000, SDS-PAGE
65000
-
2 * 65000, treatment with 2-mercaptoethanol results in 2 new bands, an A chain of 38000 Da and an B chain of 28000 Da, SDS-PAGE
70000
-
2 * 70000, 70000 Da subunit consists of 2 polypeptide chains of 30000 and 40000 Da respectively
70000
-
4 * 70000, tetramer with D2 symmetry, crystal structure and SDS-PAGE, present as dimer in solution. Each subunit is built up by three domains arranged sequentially on the polypeptide chain and tightly associated in space. The folding of all three domains is of a similar beta-barrel type, analysis of intra- and intertetramer hydrogen bond and van der Waals interactions, domains structures, detailed overview
Results 1 - 10 of 22 > >>