@article{oai:mie-u.repo.nii.ac.jp:00005745,
 author = {Okumura, Katsuzumi and 奥村, 克純 and Miyake, Yoshiaki and 三宅, 義明 and Taguchi, Hiroshi and 田口, 寛 and Shimabayashi, Yoshihide and 嶋林, 幸英},
 journal = {三重大学生物資源学部紀要 = The bulletin of the Faculty of Bioresources, Mie University},
 month = {Mar},
 note = {application/pdf, Protein disulfide-isomerase (PDI) is associated with the refolding of proteins that have mis-matched disulfide bonds through the thiol-disulfide interchange reaction. When the enzyme activity with reduced denatured RNase as the substrate was plotted for analysis of the first-order kinetics, the accelerated regeneration of RNase activity gave linear plots for both the PDI concentration and reaction time. This estimation method is simple and can be used with the values which show high regeneration of RNase activity (90%), so it should be suitable for the investigation of PDI inhibitors and inhibitors of protein refolding, and for research into the refolding process of other protein substrates, such as recombinant proteins., Protein Disulfide-isomerase （PDI） は，thiol・disulfide交換反応により誤ったdisulfide結合を持つタンパク質のrefoldingを促進する。本酵素の基質として還元変性RNaseを用い，その活性の全体的な復元過程をfirst-order kineticsによりプロットしたところ，PDI濃度並びに反応時間の両者について直線関係が得られた。この評価法は，簡単で，高いrefolding値（約90％）まで包括することから，遺伝子組換えタンパク質をはじめとする様々のタンパク質のrefoldingに対するPDIの効果の解析，並びに，PDIの阻客剤およびタンパク質のrefoldingに対する阻害因子の検討な
どに有効な方法と考えられる。},
 pages = {59--63},
 title = {Estimation of Protein Disulfide-isomerase Activity : Based on Protein Refolding},
 volume = {8},
 year = {1992}
}