16.Ni(CO)_4のネズミRNAにたいするOrA-^<14>Cのとりこみ阻害

概要

論文の詳細を見る
The lipoamide hydrolyzing enzyme, widely distributed in rat tissues, has been selectively solubilized and 4.4-fold purified from the particulate fraction of liver by Triton X-100 treatment of sonicated precipitate. It was found that the enzyme was able to decrease the over all activity of α-ketoglutarate dehydrogenase complex, partially purified from beef heart muscle. The enzyme has been more purified 7.2-fold by twice DEAE-sephadex column chromatographies. It was also demonstrated that the release of lipoic acid by purified enzyme was accompanied by the decrease of over all α-ketoglutarate dehydrogenase complex activity by the purified enzyme, although α-ketoglutarate dehydrogenase activity was remained constant. From these observations, it was concluded that the purified enzyme and lipoamidase was identical.
日本ビタミン学会の論文
1970-03-25