Sine J P, Colas B
Biochimie. 1987 Jan;69(1):75-80. doi: 10.1016/0300-9084(87)90274-4.
A soluble form of acetylcholinesterase was shown to be present in rabbit enterocytes. The enzyme was obtained from a high-speed supernatant (105,000 X g centrifugation) after homogenization of intestinal mucosa without detergent. It was shown to possess no obvious hydrophobic character and could be classified as a low-salt-soluble (LSS) acetylcholinesterase. Sucrose gradient centrifugation revealed a single enzyme species with a sedimentation coefficient of 3.9 +/- 0.2S. By gel filtration performed in HPLC the enzyme was eluted as a protein corresponding to an Mr of 72,000 +/- 3,000. It could be precipitated with concanavalin A by affinoelectrophoresis, but the catalytic activity was not affected by the lectin. Our results are consistent with a G1 globular form for this soluble acetylcholinesterase which differs very clearly from detergent-soluble forms also found recently in the plasma membranes of rabbit enterocytes.
已证明兔肠上皮细胞中存在一种可溶性乙酰胆碱酯酶。该酶是在不使用去污剂的情况下对肠黏膜进行匀浆后，从高速上清液（105,000×g离心）中获得的。结果表明，它没有明显的疏水特性，可归类为低盐溶性（LSS）乙酰胆碱酯酶。蔗糖梯度离心显示有单一的酶种类，沉降系数为3.9±0.2S。通过高效液相色谱法进行的凝胶过滤，该酶作为一种Mr为72,000±3,000的蛋白质被洗脱出来。它可通过亲和电泳用伴刀豆球蛋白A沉淀，但催化活性不受该凝集素影响。我们的结果与这种可溶性乙酰胆碱酯酶的G1球状形式一致，这与最近在兔肠上皮细胞质膜中发现的去污剂可溶性形式有明显不同。
