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The solubilization of a glucuronyltransferase involved in pea (Pisum sativum var. Alaska) glucuronoxylan synthesis.

https://arctichealth.org/en/permalink/ahliterature12264
Source
Biochem J. 1989 Dec 15;264(3):643-9
Publication Type
Article
Date
Dec-15-1989
Author
K W Waldron
E A Baydoun
C T Brett
Author Affiliation
AFRC Institute of Food Research, Norwich, U.K.
Source
Biochem J. 1989 Dec 15;264(3):643-9
Date
Dec-15-1989
Language
English
Publication Type
Article
Keywords
Carbon Radioisotopes
Chromatography, Gel
Detergents - pharmacology
Fabaceae - enzymology
Glucuronosyltransferase - isolation & purification - metabolism
Kinetics
Manganese - pharmacology
Molecular Weight
Octoxynol
Plants, Medicinal
Polyethylene Glycols - pharmacology
Polysaccharides - biosynthesis
Radioisotope Dilution Technique
Research Support, Non-U.S. Gov't
Uridine Diphosphate Glucuronic Acid - metabolism
Uridine Diphosphate Xylose - metabolism
Xylans - biosynthesis
Abstract
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.
PubMed ID
2515849 View in PubMed
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