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Xenobiotica. 1991 Feb;21(2):171-7.

Human liver sulphotransferase and UDP-glucuronosyltransferase: structure-activity relationship for phenolic substrates.

Author information

1
Department of Experimental Biomedicine, Medical School, University of Pisa, Italy.

Abstract

1. Human liver sulphotransferase and UDP-glucuronosyltransferase were studied with phenol, methyl-, ethyl-, propyl-, butyl-, phenyl-, nitro-, amino-phenols and hydroxybenzoic acids as substrates. 2. The Michaelis-Menten constants (Km) and the maximum velocities of reaction (Vmax) of sulphotransferase and UDP-glucuronosyltransferase for each substrate were measured. 3. The Km values for sulphotransferase varied over 5000-fold whereas they varied over 25-fold for UDP-glucuronosyltransferase. 4. Sulphotransferase and UDP-glucuronosyltransferase have different structure-activity relationships with phenolic substrates.

PMID:
1905436
DOI:
10.3109/00498259109039459
[Indexed for MEDLINE]

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