Ishii K, Sagami H, Ogura K
J Biochem. 1983 Jun;93(6):1635-9. doi: 10.1093/oxfordjournals.jbchem.a134302.
The microsomes from pig liver contained farnesyl pyrophosphate synthetase and it was solubilized with Triton X-100. The microsomal enzyme had a pH optimum of 6.5-7.0 and required Mg2+ or Mn2+ for maximum activity. Dimethylallyl-transferring activity of the enzyme was much lower compared with the geranyl-transferring activity. In the presence of Triton X-100, the geranyl-transferring activity was about two-fold activated whereas the dimethylallyl-transferring activity was almost the same.
猪肝微粒体含有法尼基焦磷酸合成酶,并用Triton X-100使其溶解。微粒体酶的最适pH为6.5 - 7.0,最大活性需要Mg2+或Mn2+。与香叶基转移活性相比,该酶的二甲基烯丙基转移活性要低得多。在Triton X-100存在的情况下,香叶基转移活性被激活了约两倍,而二甲基烯丙基转移活性几乎不变。