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Abstract
Highly-active purified UDP-glucuronyltransferase from guinea-pig liver microsomal membranes is associated with phospholipids. Removal of these phospholipids inactivated the transferase and caused profound changes in the enzyme's circular dichroism spectrum indicating that its secondary structure was drastically altered. Treatment of the delipidated fraction with phosphatidylcholine restored the enzyme to a much more helical, high reactivity conformation. These results show clearly that an intact phospholipid environment is required to maintain the transferase in a reactive conformation.
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