Studies on bilirubin UDP-glucuronyltransferase

Elias Halac, Albert Reff

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

The capacity of liver fractions to conjugate bilirubin and p-nitrophenol with glucuronic acid is increased several fold by dialysis against alkaline EDTA. UDPglucuronyltransferase (UDP-glucuronate glucuronyltransferase (acceptor-unspecific), EC 2.4.1.17), with activity towards bilirubin and p-nitrophenol, has been solubilized by treating microsomes activated with EDTA and deoxycholate. Kinetic data obtained with activated microsomes, and fractionation and inactivation experiments performed with deoxycholate-solubilized enzyme have yielded evidence in favor of the existence of at least two UDP-glucuronyltransferases. Microsomal pellets were examined by electron microscopy before EDTA, after EDTA, and after EDTA and deoxycholate. The most apparent change that is concomitant with the activation by EDTA is the transformation of rough membranes into smooth membranes.

Original languageEnglish
Pages (from-to)328-343
Number of pages16
JournalBBA - Enzymology
Volume139
Issue number2
DOIs
StatePublished - 11 Jul 1967
Externally publishedYes

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