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PLANT BIOCHEMISTRY OF XENOBIOTICS - ISOLATION AND CHARACTERIZATION OF A SOYBEAN O-GLUCOSYLTRANSFERASE OF DDT METABOLISM
Author(s): WETZEL A, SANDERMANN H
Source: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS    Volume: 314    Issue: 2    Pages: 323-328    Published: NOV 1 1994  
Times Cited: 22     References: 24     
Abstract: The insecticide DDT is metabolized in soybean and wheat cell cultures to the acylglucoside of 2,2-bis-(4-chlorophenyl)-acetic acid (DDA) (M. Arjmand and H. Sandermann, 1985, Pesticide Biochem. Physiol. 23, 389-397). An enzyme catalyzing the conjugation reaction has been highly purified from the soluble enzyme fraction of cultured soybean cells. After the initial ammonium sulfate fractionation, quercetin and pentachlorophenol were preferentially glucosylated. In the course of 367-fold purification, DDA became the preferred substrate. The purified enzyme was unstable. A molecular weight of similar to 50 kDa was estimated for the native enzyme (gel permeation chromatography) as well as the denatured protein (sodium dodecyl sulfate-gel electrophoresis). The isoelectric point for the enzyme was near pH 4.9. Apparent K-m values of about 170 mu M were determined for UDP-glucose as well as DDA. The maximal velocity was 257 mu kat/kg protein, corresponding to a conjugation capacity of 855 mu g DDA/h/g fresh weight of cells. (C) 1994 Academic Press,Inc.
Document Type: Article
Language: English
Addresses:
1. GSF FORSCHUNGSZENTRUM UNWELT & GESUNDHEIT GMBH, INST BIOCHEM PFLANZENPATHOL, D-85758 OBERSCHLEISSHEIM, GERMANY
Publisher: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495
Subject Category: Biochemistry & Molecular Biology; Biophysics
IDS Number: PN866
ISSN: 0003-9861
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