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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-8-20
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pubmed:abstractText |
Rat renal microsomes catalyzed the glucuronidation of l-naphthol, 4-methylumbelliferone and p-nitrophenol, whereas morphine and testosterone conjugation were not detected. In contrast, all five substrates were conjugated by hepatic microsomes; the activity was typically 5-10 times greater than with renal microsomes. Renal microsomal UDP-glucuronyltransferase toward l-naphthol was fully activated (six-fold) by 0.03% deoxycholate while the hepatic enzyme was fully activated (eight-fold) by 0.05% deoxycholate. Full activation of hepatic UDP-glucuronyltransferase occurred when microsomes had been preincubated at 0 C with deoxycholate for 20 min. This effect of preincubation was not observed with renal microsomes. The presence of 0.25M sucrose in the buffers during renal microsomal preparation resulted in a two-fold greater rate of l-naphthol conjugation in both unactivated and activated microsomes than renal microsomes prepared in phosphate buffers alone. Preparation of hepatic microsomes with or without 0.25M sucrose had no effect on UDP-glucuronyltransferase activity. Unactivated (-deoxycholate) renal enzyme was activated when incubations were done at a low pH (5.7), whereas fully activated (0.03% deoxycholate) renal microsomal UDP-glucuronyltransferase displayed a pH optimum at 6.5. Renal microsomal UDP-glucuronyltransferase activity toward l-naphthol, p-nitrophenol and 4-methylumbelliferone was induced by pretreatment of rats with beta-naphthoflavone and trans-stilbene oxide but not by phenobarbital or 3-methylcholanthrene. These data demonstrate that renal UDP-glucuronyltransferases are different from the hepatic enzymes with regard to biochemical properties, substrate specificity and in response to chemical inducers of xenobiotic metabolism.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aryl Hydrocarbon Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronates,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Phenobarbital,
http://linkedlifedata.com/resource/pubmed/chemical/Sucrose,
http://linkedlifedata.com/resource/pubmed/chemical/naphthyl glucuronide
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0024-3205
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-53
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:6429466-Animals,
pubmed-meshheading:6429466-Aryl Hydrocarbon Hydroxylases,
pubmed-meshheading:6429466-Glucuronates,
pubmed-meshheading:6429466-Glucuronosyltransferase,
pubmed-meshheading:6429466-Hydrogen-Ion Concentration,
pubmed-meshheading:6429466-Kidney Cortex,
pubmed-meshheading:6429466-Male,
pubmed-meshheading:6429466-Microsomes,
pubmed-meshheading:6429466-Microsomes, Liver,
pubmed-meshheading:6429466-Phenobarbital,
pubmed-meshheading:6429466-Rats,
pubmed-meshheading:6429466-Rats, Inbred F344,
pubmed-meshheading:6429466-Sucrose,
pubmed-meshheading:6429466-Time Factors
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pubmed:year |
1984
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pubmed:articleTitle |
Characteristics of renal UDP-glucuronyltransferase.
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pubmed:publicationType |
Journal Article
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