A glucuronyltransferase involved in glucuronoxylan biosynthesis was obtained from the epicotyls of 1-week-old etiolated pea (Pisum sativum var. Alaska) seedlings and was solubilized in Triton X-100, a non-ionic detergent. The enzyme was inactivated by SDS and inhibited by Derriphat 160 and cholic acid. The enzyme was active in the presence of NN-dimethyldodecylanium-N-oxide, but was not solubilized by it. The stimulatory effect of UDP-D-xylose on the particulate and solubilized enzymes was the same, but the optimum Mn2+ concentration was lower for the solubilized enzyme, and the product formed by the solubilized enzyme has altered structure and solubility properties. Gel filtration of the solubilized enzyme on Sepharose CL-6B permitted partial separation of the stimulatory effect of UDP-D-xylose from the activity in the absence of UDP-D-xylose. The solubilized enzyme was more stable than the particulate enzyme and could be stored for 2 weeks at -20 degrees C without loss of activity.
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Research Article|
December 15 1989
The solubilization of a glucuronyltransferase involved in pea (Pisum sativum var. Alaska) glucuronoxylan synthesis
K W Waldron;
K W Waldron
*AFRC Institute of Food Research, Colney Lane, Norwich NR4 7UA, U.K.
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E A H Baydoun;
E A H Baydoun
†Department of Biology, American University of Beirut, Beirut, Lebanon
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C T Brett
C T Brett
‡Plant Molecular Science Group, Department of Botany, University of Glasgow, Glasgow G12 8QQ, Scotland, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1989 London: The Biochemical Society
1989
Biochem J (1989) 264 (3): 643–649.
Citation
K W Waldron, E A H Baydoun, C T Brett; The solubilization of a glucuronyltransferase involved in pea (Pisum sativum var. Alaska) glucuronoxylan synthesis. Biochem J 15 December 1989; 264 (3): 643–649. doi: https://doi.org/10.1042/bj2640643
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