Abstract：
:Bispecific O-methyltransferase (OMT, EC 2.1.1.68) which catalyses the meta-specific methylation of caffeic acid and 5-hydroxyferulic acid was purified to homogeneity from the developing secondary xylem of aspen (Populus tremuloides). The enzyme was purified by conventional techniques and affinity chromatography on S-adenosyl-L-homocysteine agarose using substrate elution. The enzyme has a M(r) of 40,000 as determined by SDS-PAGE. Amino acid sequences of three peptides produced from a proteolytic digest of bispecific OMT were obtained by automated Edman degradation. Polyclonal antibodies raised against the purified OMT reacted strongly to OMT in both purified and unpurified fractions in western blots. Addition of an equal concentration of anti-OMT IgG to crude extract protein inhibited OMT activity by more than 70%.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Bugos RC,Chiang VL,Campbell WHdoi
10.1016/0031-9422(92)83093-esubject
Has Abstractpub_date
1992-05-01 00:00:00pages
1495-8issue
5eissn
0031-9422issn
1873-3700pii
0031-9422(92)83093-Ejournal_volume
31pub_type
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