Characterization of bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase from aspen

Authors

R.C. Bugos
V.L.C. Chiang
W.H. Campbell

Document Type

Article

Journal/Book Title/Conference

Phytochemistry

Volume

31

Issue

5

First Page

1495

Last Page

1498

Publication Date

1992

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 Mr 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%.

Recommended Citation

Bugos, R. C.; Chiang, V. L. C.; Campbell, W. H. 1992. Characterization of bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase from aspen. Phytochemistry. 31 (5): 1495-1992.