1. The glucuronide conjugation of @entity11921 , @entity18888 , @entity70495 and @entity11108 by @entity35 liver microsomes has been studied. The detergent Triton X-100 activated @entity858 -glucuronyltransferase activity towards all these substrates, therefore the optimum activating concentration was added in all experiments. 2. @entity1025 enhanced the conjugation of the substrates. 3. With @entity18888 substrate inhibition occurred but this could be relieved by adding albumin, which binds excess of @entity18888 . 4. Kinetic constants of the substrates and @entity858 - @entity8686 have been determined. Mutual inhibition was found with the substrates @entity11921 , @entity11108 and @entity18888 . @entity11921 conjugation was inhibited competitively by @entity18888 and @entity11108 . 5. @entity70495 did not inhibit the conjugation of the other three substrates because these are conjugated preferentially to @entity70495 . 6. It is concluded that the four substrates are conjugated by one enzyme at the same active site.

The heterogeneity of @entity858 glucuronyltransferase from XXXX liver.

@entity1025 :: ('CHEBI:18420', 'Chemical') :: ['Mg(2+)'] @entity18888 :: ('MESH:D020113', 'Chemical') :: ['phenolphthalein'] @entity858 :: ('MESH:D014530', 'Chemical') :: ['UDP'] @entity11108 :: ('MESH:C489431', 'Chemical') :: ['4-methylumbelliferone'] @entity8686 :: ('MESH:D020723', 'Chemical') :: ['glucuronate'] @entity35 :: ('10116', 'Species') :: ['rat'] @entity11921 :: ('MESH:C024836', 'Chemical') :: ['p-nitrophenol', 'p-Nitrophenol'] @entity70495 :: ('MESH:C027667', 'Chemical') :: ['o-aminophenol', 'o-Aminophenol']
@entity35 :: (10116,Species) :: ['rat']
