書誌事項
- タイトル別名
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- Studies on the Metabolic Fate of TA-510, a Hepatic Anti-inflammatory Agent. (III).Ildentitication of TA-510 Reductase in Human Liver.
- : Identification of TA-510 Reductase in Human Liver
- : ヒト肝臓におけるTA-510還元酵素の同定
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抄録
To identify TA-510 reductase and obtain information on the stereochemical aspects, the reductase activity has been studied in subcellular fractions from 15 human livers, and finally purified using TA-510 enantiomers as substrates.<BR> 1. This activity was present in the cytosolic fraction and exhibited strong product stereoselectivity, i.e. both enantiomers were reduced exclusively to trans-alcohol (M1), but not cis-alcohol. Human liver microsomes showed practically no ketone reductase activity.<BR> 2. There was also a remarkable variation between the subjects in the substrate stereoselectivity, suggesting that racemic TA-510 was metabolized by at least two reductive enzymes with different stereochemical requirements.<BR> 3. The enzyme responsible for the reduction of (+)-TA-510 enantiomer was co-eluted with carbonyl reductase during purification steps, and separated from another enzyme with preference to (-)-TA-510 enantiomer as a substrate. Identity of (+) -TA-510 reductase and carbonyl reductase was also suggested by comparing the kinetic analysis and susceptibility to inhibitors of human liver cytosols and the purified enzyme.<BR> 4. (-)-TA-510 reductase was purified to a homogeneous protein and was shown as a monomeric protein with a molecular weight of 36 kDa. Amino acid sequences of five peptides obtained by proteolytic digestion of the purified enzyme were completely identical to the corresponding regions of previously reported 3α-hydroxysteroid/dihydrodiol dehydrogenase.
収録刊行物
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- 薬物動態
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薬物動態 15 (4), 338-348, 2000
日本薬物動態学会
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詳細情報 詳細情報について
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- CRID
- 1390001204669389696
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- NII論文ID
- 10008416423
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- NII書誌ID
- AN10144117
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- ISSN
- 09161139
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可