De Jong B J, Kalkman C, Hülsmann W C
Biochim Biophys Acta. 1978 Jul 25;530(1):56-66. doi: 10.1016/0005-2760(78)90126-1.
In intestinal epithelial cells, three enzymes possessing monoacylglycerol hydrolase activity were found and partially purified. Two of these enzymes have properties that justify their classification as an esterase and one as a monoacylglycerol lipase. The three enzymes show similar Km values for monooleoylglycerol and each shows similar activity towards 1- and 2-monopalmitoylglycerol. Antiserum raised in rabbits against rat liver monoacylglycerol lipase inhibits the intestinal lipase completely, suggesting that the enzymes are at least partially similar. The esterases of small intestinal villus cells were not inhibited by the antiserum against liver monoacylglycerol lipase. It was calculated that the esterases account for approx. 2/3 of the monooleoylglycerol hydrolase activity in epithelial cells. Monoacylglycerol lipase also hydrolyzed palmitoyl-CoA, while the esterases did not. The enzymes were inhibited by micellar palmitoyl-CoA. The hypothesis that palmitoyl-CoA is an important regulator for monoacylglycerol acylation is discussed in the light of these new findings.
在肠上皮细胞中，发现了三种具有单酰甘油水解酶活性的酶，并对其进行了部分纯化。其中两种酶的特性使其可归类为酯酶，另一种则归类为单酰甘油脂肪酶。这三种酶对单油酰甘油的Km值相似，并且对1-和2-单棕榈酰甘油均表现出相似的活性。用兔抗大鼠肝脏单酰甘油脂肪酶制备的抗血清可完全抑制肠脂肪酶，这表明这些酶至少部分相似。小肠绒毛细胞的酯酶不受抗肝脏单酰甘油脂肪酶的抗血清抑制。据计算，酯酶约占上皮细胞中单油酰甘油水解酶活性的2/3。单酰甘油脂肪酶也能水解棕榈酰辅酶A，而酯酶则不能。这些酶受到胶束棕榈酰辅酶A的抑制。根据这些新发现，讨论了棕榈酰辅酶A是单酰甘油酰化重要调节剂的假说。
