Abstract
UDP-glucose: 4-hydroxybenzoate glucosyltransferase (4HB glucosyltransferase, EC 2.4.1.194) was purified to near homogeneity from cell suspension cultures of Lithospermum erythrorhizon, using ammonium sulphate precipitation, and column chromatography on DEAE Sephacel, Superdex 200, hydroxyapatite, HiTrap blue, Mono P and Mono Q. Affinity chromatography on HiTrap blue was the crucial step for the success of this scheme. After removal of NAD-dependent enzymes from the HiTrap blue column with NAD (5 mM), the 4HB glucosyltransferase was eluted specifically with UDP-glucose (0–20 mM). The above purification procedure resulted in an enzyme fraction with 27 300-fold higher specific 4HB glucosyltransferase activity than the crude enzyme extract. The enzyme is a monomer of about M r , 51 k, determined by SDS-PAGE. © 1997 Published by Elsevier Science Ltd. All rights reserved
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