dimer
1 * 31000 + 1 * 95000, SDS-PAGE
monomer
1 * 40000, SDS-PAGE
monomer
1 * 49000, SDS-PAGE
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isolated methyltransferase domain shows a lower but kinetically equivalent activity than the complete enzyme, which is highly enhanced by association with the D12 subunit
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primary sequence, sequence comparison with other species, enzyme-ligand structures
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subunit organisation of the mRNA capping enzyme complex
heterodimer
the guanine-N7 methyltransferase domain of vaccinia virus mRNA capping enzyme is a heterodimer composed of a catalytic subunit and a stimulatory subunit, X-ray crystallography
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the methyl/guanylyltransferase complex on vaccinia virus dissociates into two subunits of MW 31400 and 95000 by action of SDS-PAGE
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x * 39000, SDS-PAGE of His-tagged TbCmt1