| pubmed-article:1638515 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C0001734 | lld:lifeskim |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C0017817 | lld:lifeskim |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C1160466 | lld:lifeskim |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C2825097 | lld:lifeskim |
| pubmed-article:1638515 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:1638515 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1638515 | pubmed:dateCreated | 1992-9-2 | lld:pubmed |
| pubmed-article:1638515 | pubmed:abstractText | Glutathione (GSH) conjugation of microsome-mediated and synthetic aflatoxin B1 (AFB1)-epoxide and styrene oxide has been investigated with purified GSH S-transferases (GSTs) from rats. Both styrene oxide and AFB1-epoxide were conjugated preferentially by millimicrons GSTs 3-3, 3-4 and 4-4 as compared to alpha GSTs 1-1, 1-2 and 2-2. The highest catalytic activity with styrene oxide conjugation was associated with GST 4-4. The highest catalytic activity with microsome-mediated AFB1-epoxide conjugation was observed with GST 3-3 whereas with the synthetic AFB1-epoxide conjugation was seen with GST 4-4. The catalytic activity of pi GST 7-7 was intermediate to millimicrons and alpha GSTs. It is suggested that GST 3-3 may play an important role in inactivation of AFB1-epoxide generated in vivo in the rat. | lld:pubmed |
| pubmed-article:1638515 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1638515 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1638515 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1638515 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1638515 | pubmed:issn | 0304-3835 | lld:pubmed |
| pubmed-article:1638515 | pubmed:author | pubmed-author:LotlikarP DPD | lld:pubmed |
| pubmed-article:1638515 | pubmed:author | pubmed-author:JensenD EDE | lld:pubmed |
| pubmed-article:1638515 | pubmed:author | pubmed-author:GopalanPP | lld:pubmed |
| pubmed-article:1638515 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1638515 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:1638515 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:1638515 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1638515 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1638515 | pubmed:pagination | 225-33 | lld:pubmed |
| pubmed-article:1638515 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:meshHeading | pubmed-meshheading:1638515-... | lld:pubmed |
| pubmed-article:1638515 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1638515 | pubmed:articleTitle | Glutathione conjugation of microsome-mediated and synthetic aflatoxin B1-8,9-oxide by purified glutathione S-transferases from rats. | lld:pubmed |
| pubmed-article:1638515 | pubmed:affiliation | Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA. | lld:pubmed |
| pubmed-article:1638515 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1638515 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1638515 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
