pubmed-article:6429466 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6429466 | lifeskim:mentions | umls-concept:C0022646 | lld:lifeskim |
pubmed-article:6429466 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
pubmed-article:6429466 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:6429466 | pubmed:dateCreated | 1984-8-20 | lld:pubmed |
pubmed-article:6429466 | 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. | lld:pubmed |
pubmed-article:6429466 | pubmed:language | eng | lld:pubmed |
pubmed-article:6429466 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6429466 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6429466 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6429466 | pubmed:month | Jul | lld:pubmed |
pubmed-article:6429466 | pubmed:issn | 0024-3205 | lld:pubmed |
pubmed-article:6429466 | pubmed:author | pubmed-author:HookJ BJB | lld:pubmed |
pubmed-article:6429466 | pubmed:author | pubmed-author:RushG FGF | lld:pubmed |
pubmed-article:6429466 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6429466 | pubmed:day | 9 | lld:pubmed |
pubmed-article:6429466 | pubmed:volume | 35 | lld:pubmed |
pubmed-article:6429466 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6429466 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6429466 | pubmed:pagination | 145-53 | lld:pubmed |
pubmed-article:6429466 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
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pubmed-article:6429466 | pubmed:year | 1984 | lld:pubmed |
pubmed-article:6429466 | pubmed:articleTitle | Characteristics of renal UDP-glucuronyltransferase. | lld:pubmed |
pubmed-article:6429466 | pubmed:publicationType | Journal Article | lld:pubmed |