A Study on Thermostability of Immobilized Uridine Diphosphate-Glucouronyltransferase

Toshio NANBO; Shin-ichi NINOMIYA; Masao YONEYAMA

doi:10.1248/cpb.40.823

著者情報

キーワード: immobilization, microsome solubilization, uridine diphosphate-glucuronyltransferase, thermostability, fluorescence polarization, thermodynamic parameter

ジャーナルフリー

1992 年 40 巻 3 号 p. 823-825

DOI https://doi.org/10.1248/cpb.40.823

詳細

抄録

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°C. 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°C. The influence of immobilization on thermostability of UDPGT is discussed.

責任著者(Corresponding author)

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