@article{oai:niigata-u.repo.nii.ac.jp:00023365, author = {岩田, 豊人}, issue = {8}, journal = {新潟医学会雑誌, 新潟医学会雑誌}, month = {Aug}, note = {ATP: sn-1, 2-diacylglycerol phosphotransferase [EC 2.7.1.-., DG-kinase] was purified from pig thymus cytosol. The activity of the enzyme was reconstituted by the addition of either deoxycholate or phosphatidylcholine (PC). In addition, bovine serum albumin also activated DG-kinase activity. As was seen in the activation kinetics by PC alone, polymyxin B at 4μM in the presence of PC activated DG-kinase by increasing the number of activated enzyme. On the other hand, polymyxin B at 10μM inhibited DG-kinase by altering the interaction between 1,2-diacylglycerol and detergent. Similar inhibition was also observed by the addition of oleoyl CoA. Since oleoyl-CoA is a substrate of triacylglycerol synthesis, inhibitory effect of oleoyl-CoA on DG-kinase may play a regulatory role in vivo. Ca^<2+> at 10^<-7> M inhibited DG-kinase activity, suggesting a possible role of Ca^<2+> in modulation of DG-kinase activity in vivo. The inhibitory effect of p-mercuribenzoate on DG-kinase activity was partially relieved by the addition of dithiothreitol, indicating that the inhibition might be reversible. As compared with 1,3-diaclyglycerol, preincubation of DG-kinase with 1,2-diacylglycerol effectively protected p-mercuribenzoate inhibition. These observations suggest that DG-kinase may have a functional SH-group and can be regulated through hydrophobic interaction, oleoyl-CoA and Ca^<2+> in the process of biomembrane response systems.}, pages = {501--509}, title = {豚胸腺より精製したsn-1,2-ジアシルグリセロールキナーゼ活性の再構成}, volume = {102}, year = {1988} }