A Study on Thermostability of Immobilized Uridine Diphosphate-Glucouronyltransferase
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概要
- 論文の詳細を見る
Uridine diphosphate-glucuronyltransferase (UDPGT) in the hepatic microsome of the rat was solubilized with Emulgen 911 and then immobilized on agarose. The thermostability of immobilized UDPGT was compared with solubilized UDPGT and was found to be higher at temperatures above 52.5℃. The activation energy (E_a) for thermoinactivation was lowered by immobilization. THe fluorescence polarization of tryptophanyl residue of immobilized protein showed littele change compared with solubilized protein when heated to 54℃. The influence of immobilization on thermostability of UDPGT is discussed.
- 公益社団法人日本薬学会の論文
- 1992-03-25
著者
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南保 俊雄
Tokai Research Laboratories Daiichi Pure Chemicals Co. Ltd.
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二宮 真一
Tokai Research Laboratories Daiichi Pure Chemicals Co. Ltd.
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米山 政男
Tokai Research Laboratories, Daiichi Pure Chemicals Co., Ltd.
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米山 政男
Tokai Research Laboratories Daiichi Pure Chemicals Co. Ltd.
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