Négrel R, Serrero G, Fernandez-Lopez V, Ailhaud G
Eur J Biochem. 1976 Dec;71(1):249-58. doi: 10.1111/j.1432-1033.1976.tb11111.x.
The preferential cellular distribution in the villus tip and the subcellular localization in the endoplasmic reticulum of an intestinal glycerol-ester hydrolase from rat mucosa are described. The enzyme is shown not to be from either pancreatic or bacterial origin; it catalyzes the hydrolysis of short- and medium chain triglycerides and of p-nitrophenylacetate. Contrarily to the specificity found for the pig intestinal lipase (Serrero, Négrel and Ailhaud, 1975), no activity is detectable against acylCoA; a thiolester hydrolase different from the glycerol-ester hydrolase was demonstrated after differential solubilization and chromatographic separation. A high proportion of glycerol-ester hydrolase is present in the intestinal lumen; its possible complementary role in lipid degradation is discussed.
本文描述了大鼠粘膜肠甘油酯水解酶在绒毛顶端的优先细胞分布以及在内质网中的亚细胞定位。该酶并非源自胰腺或细菌；它催化短链和中链甘油三酯以及对硝基苯乙酸酯的水解。与猪肠脂肪酶的特异性（Serrero、Négrel和Ailhaud，1975年）不同，对酰基辅酶A未检测到活性；经差异溶解和色谱分离后，证明存在一种不同于甘油酯水解酶的硫酯水解酶。肠腔中存在高比例的甘油酯水解酶；讨论了其在脂质降解中可能的互补作用。
