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. 1991 Jul;288(1):302-9.
doi: 10.1016/0003-9861(91)90199-s.

Purification and immunocharacterization of a plant cytochrome P450: the cinnamic acid 4-hydroxylase

B Gabriac  1 , D Werck-Reichhart, H Teutsch, F Durst
Affiliations

Purification and immunocharacterization of a plant cytochrome P450: the cinnamic acid 4-hydroxylase

B Gabriac et al. Arch Biochem Biophys. 1991 Jul.

Abstract

Cinnamic acid 4-hydroxylase (CA4H) was purified from microsomes of manganese-induced Jerusalem artichoke (Helianthus tuberosus L.) tuber tissues. The three-step purification procedure involved solubilization and phase partitioning in Triton X-114, followed by chromatography on DEAE-Trisacryl and hydroxylapatite columns. Purification was monitored using carbon monoxide and type I substrate binding properties of the enzyme. The protein, purified to electrophoretic homogeneity, showed an Mr of about 57,000 on SDS-PAGE. Polyclonal antibodies raised against this protein selectively reacted with a 57-kDa polypeptide on Western blots of induced Jerusalem artichoke microsomes. The antibody selectively and strongly inhibited CA4H activity from several plant species.

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