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EC Number Subunits Commentary Reference
Show all pathways known for 2.1.1.28Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.28dimer gel filtration reveals the presence of two species at elution volumes consistent with monomeric and dimeric human phenylethanolamine N-methyltransferase. The more prominent peak corresponds to the dimer form. The amount of dimer can be reduced either by using a more elute concentration of the protein or by the addition of 0.5 mM DTT to the running buffer. SDS-PAGE can not distinguish between the two forms. Native PAGE clearly distinguishes between the two forms of human phenylethanolamine N-methyltransferase. Crystals from the dimer fraction grow faster. Monomer and dimer human phenylethanolamine N-methyltransferase have similar kinetic constatns. The monomer-dimer equilibruim in analytical ultracentrifugation for the dimer frations of phenylethanolamine N-methyltransferase-His and C48A phenylethanolamine N-methyltransferase is 10fold lower than for the monomer fractions (Kd 35-64 microM and 305-551 microM, respectively). 672345
Show all pathways known for 2.1.1.28Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.28monomer 1 * 35000, enzyme form E-3, SDS-PAGE 639434
Show all pathways known for 2.1.1.28Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.28monomer 1 * 40000, enzyme form E-1, SDS-PAGE 639434
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