Studies on a solubilized oestriol 16α-glucuronyltransferase from human liver microsomes

Rao, Govind S.; Rao, Marie Luise; Breuer, H.

doi:10.1016/0022-4731(72)90005-2

Journal of Steroid Biochemistry

1972

DOI: 10.1016/0022-4731(72)90005-2

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Studies on a solubilized oestriol 16α-glucuronyltransferase from human liver microsomes

Govind S. Rao

Marie Luise Rao

H. Breuer

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1973

1979

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Cited by 10 publications

(1 citation statement)

References 18 publications

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“…Subsequently, Graham et al (1977), by using a similar gel-filtration method to remove phospholipids, was able to restore p-nitrophenol glucuronyltransferase activity if the detergent in the preparation was removed by Bio-Beads in the presence of phospholipids. Rao et al (1972) have shown that phospholipids are capable of restoring * To whom reprint requests should be sent.…”

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confidence: 99%

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

Tukey¹,

Billings²,

Autor³

et al. 1979

Biochemical Journal

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Hepatic UDP-glucuronyltransferase activity was resolved into two fractions, one exhibiting oestrone glucuronyltransferase activity and the other exhibiting p-nitrophenol glucuronyltransferase activity. Hydroxyapatite-column chromatography removed greater than 95 % of the phospholipids from both preparations. The partially purified delipidated enzymes were essentially devoid of catalytic activity, but activities were restored by the addition of phospholipids or phosphatidylcholine mixtures containing various saturated and unsaturated fatty acids. Both oestrone andp-nitrophenol glucuronyltransferase activities were reconstituted to similar degrees with the phosphatidylcholine mixtures. When purified phospholipids were tested, phosphatidylcholine and lysophosphatidylcholine were most effective in restoring activity, whereas phosphatidylethanolamine was the least effective. These results further suggest that oestrone and p-nitrophenol UDP-glucuronyltransferases are dependent on phospholipids for their activity.

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confidence: 99%

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

Tukey¹,

Billings²,

Autor³

et al. 1979

Biochemical Journal

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A problem of nomenclature (II): Freund's adjuvants

Whitehouse

1973

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Nature of the enhancement of hepatic uridine diphosphate glucuronyltransferase activity by 2,3,7,8-tetrachlorodibenzo-p-dioxin in rats

Lucier

McDaniel

Hook

1975

Biochemical Pharmacology

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Studies on a solubilized oestriol 16α-glucuronyltransferase from human liver microsomes

Cited by 10 publications

References 18 publications

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

A problem of nomenclature (II): Freund's adjuvants

Nature of the enhancement of hepatic uridine diphosphate glucuronyltransferase activity by 2,3,7,8-tetrachlorodibenzo-p-dioxin in rats

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