Matsuoka S, Sagami H, Kurisaki A, Ogura K
Chemical Research Institute of Non-Aqueous Solutions, Tohoku University, Sendai, Japan.
J Biol Chem. 1991 Feb 25;266(6):3464-8.
Several detergents activated microsomal dehydrodolichyl diphosphate synthase of rat liver, but the chain length of products shifted downward from C90 and C95 with increasing concentration of the detergents. Maximum activation was observed at the concentration of 2% Triton X-100, 30 mM octyl glucoside, 30 mM 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, and 10 mM deoxycholate with the product chain length being C80-C85, C65-C75, C70-C75, and C55-C65, respectively. The activity of Triton X-100 solubilized enzyme was decreased by asolectin, phosphatidylethanolamine, and phosphatidylcholine. The chain lengths of products formed in the presence of these phospholipids were C85 and C90. In the presence of both phosphatidylcholine and Mg2+ the solubilized enzyme was able to produce C90 and C95 dehydrodolichyl diphosphates like native microsomal enzyme. Microsomal enzyme preparations from rat liver, brain, and testis catalyzed the formation of dehydrodolichyl diphosphates with the same chain lengths as those of the natural dolichols occurring in individual tissues. The chain length distribution of dehydrodolichyl products by (rat liver) microsomes also depended on the concentration of substrates. Not only did increasing the concentration of isopentenyl diphosphate lead to longer chain product, but decreasing that of farnesyl diphosphate increased product chain length.
几种去污剂可激活大鼠肝脏微粒体脱氢多萜醇二磷酸合酶，但随着去污剂浓度的增加，产物的链长从C90和C95向下移动。在2% Triton X-100、30 mM辛基葡糖苷、30 mM 3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐和10 mM脱氧胆酸盐浓度下观察到最大激活，产物链长分别为C80-C85、C65-C75、C70-C75和C55-C65。Triton X-100溶解的酶的活性被大豆卵磷脂、磷脂酰乙醇胺和磷脂酰胆碱降低。在这些磷脂存在下形成的产物的链长为C85和C90。在磷脂酰胆碱和Mg2+两者存在的情况下，溶解的酶能够像天然微粒体酶一样产生C90和C95脱氢多萜醇二磷酸。来自大鼠肝脏、大脑和睾丸的微粒体制剂催化形成的脱氢多萜醇二磷酸的链长与各个组织中天然多萜醇的链长相同。（大鼠肝脏）微粒体产生的脱氢多萜醇产物的链长分布也取决于底物浓度。不仅异戊烯基二磷酸浓度的增加导致产物链长增加，而且法尼基二磷酸浓度的降低也增加了产物链长。
