Clegg R A
Biochim Biophys Acta. 1981 May 22;664(2):397-408. doi: 10.1016/0005-2760(81)90062-x.
Subcellular fractionation studies were done using lactating rat mammary tissue. Lipoprotein lipase (E.C. 3.1.1.34) was found to be associated with plasma membrane-enriched and endoplasmic reticulum-enriched fractions. Considerable amounts of soluble lipoprotein lipase were found after homogenization of this tissue. The membrane-associated lipoprotein lipase activities described here were found to be resistant to release, by heparin, from their membrane sites. Buoyant density gradient fractionation experiments suggest that the lipoprotein lipase activity of lactating mammary tissue is located in part on the secretory epithelial cell plasma membrane. This conclusion is discussed in the context of the known site of action, in vivo, of mammary gland lipoprotein lipase, and of probable routes of its transport to that site.
利用泌乳大鼠乳腺组织进行了亚细胞分级分离研究。发现脂蛋白脂肪酶（E.C. 3.1.1.34）与富含质膜和富含内质网的组分相关。在该组织匀浆后发现了相当数量的可溶性脂蛋白脂肪酶。此处描述的膜相关脂蛋白脂肪酶活性被发现对肝素从其膜位点的释放具有抗性。浮力密度梯度分级分离实验表明，泌乳乳腺组织的脂蛋白脂肪酶活性部分位于分泌上皮细胞质膜上。这一结论在乳腺脂蛋白脂肪酶在体内已知作用位点以及其转运至该位点的可能途径的背景下进行了讨论。
