Linked Life Data

3149280

Source:http://linkedlifedata.com/resource/pubmed/id/3149280

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-5-16
pubmed:abstractText
A form of UDP-glucuronyltransferase has been purified from liver microsomes of 3-methylcholanthrene-treated rats by a simple and rapid method involving chromatography on DEAE-Toyopearl and UDP-hexanolamine Sepharose columns. The purified preparation gave a single protein band (Mr 54,000) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It catalyzed the glucuronidation of not only phenolic xenobiotics such as 4-nitrophenol, 1-naphthol, and eugenol but also serotonin, which is an endogenous compound. Its activities toward 4-hydroxybiphenyl and testosterone were very low and no activity was detected toward bilirubin. After removal of the detergent (Emulgen 911), the transferase activity was stimulated by various phospholipids, about 10-fold activation being attained with phosphatidylcholine and lysophosphatidylcholine. On nitrocellulose sheets concanavalin A, but not wheat germ agglutinin, bound to the purified transferase, and this binding was abolished in the presence of alpha-methylmannoside and after treatment of the enzyme with endo-beta-N-acetylglucosaminidase H (Endo H). These observations provided evidence that the transferase is a glycoprotein carrying a "high mannose type" of oligosaccharide chain(s). The NH2-terminal 7 residues of the purified enzyme were determined to be Thr-Lys-Leu-Leu-Val-Trp-Pro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
531-6
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification and properties of a form of UDP-glucuronyltransferase from liver microsomes of 3-methylcholanthrene-treated rats.
pubmed:affiliation
Department of Veterinary Biochemistry, School of Veterinary Medicine, Rakuno Gakuen University, Hokkaido.
pubmed:publicationType
Journal Article