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J. Biochem, 1988, Vol. 104, No. 3 421-426
© 1988 Japanese Biochemical Society

research-article

Purification and Properties of 5-Hydroxytryptamine UDP-Glucuronyltransferase from Rat Liver Microsomes1

Norio Abe2, Eri Abe2 and Akira Yuasa

Department of Veterinary Biochemistry, School of Veterinary Medicine, Rakuno Gakuen University Ebetsu, Hokkaido 069

5-Hydroxytryptamine UDP-glucuronyltransferase was highly purified from untreated rat liver microsomes. The specific activity towards 5-hydroxytryptamine was increased 178-fold over the starting solubilized microsomes with a final yield of 3%. The final preparation contained two major and one minor Coomassie brilliant blue staining polypeptide bands visible after SDS-polyacrylamide gel electrophoresis. One of the major bands was identified as 3-methylcholanthrene-inducible UDP-glucuronyltransferase, so the other (molecular weight of 55,500) appeared to be 5-hydroxytryptamine UDP-glucuronyltransferase. Concanavalin A reacted with the 55,500-dalton polypeptide. Phospholipid was indispensable for the enzyme activity. The enzyme activity in the final preparation was activated by divalent cations. Simple Michaelis-Menten kinetics was followed with respect to 5-hydroxytryptamine, but deviations from this kinetics were observed with respect to UDP-glucuronic acid and Mg2+ As regards Mg2+ stimulation, further experiments indicated that the added Mg2+ was non-competitive with 5-hydroxytryptamine, but at low concentrations of Mg2+ it was competitive with UDP-glucuronic acid and at high concentrations of Mg2+ it was non-competitive with UDP-glucuronic acid. The final preparation showed high substrate specificity towards 5-hydroxytryptamine among endogenous substrates tested. From these results, it was concluded that the enzyme described here is a new form of UDP-glucuronyltransferase isozyme, and its activity showed a peculiar dependence on Mg2+.

1This study was supposed in part by a Grant-in-Aid for Scientific Research (No. 60560324) from the Ministry of Education, Science and Culture of Japan.

2Present address: Otaka Research Laboratory, Ohtaka Enzyme Company, Ltd., Otaru, Hokkaido 047-01.


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