Orlacchio A, Maffei C, Binaglia L, Porcellati G
Biochem J. 1981 May 1;195(2):383-8. doi: 10.1042/bj1950383.
The phospholipid acyl-chain dependence of the membrane-bound lysosomal beta-N-acetyl-D-glucosaminidase has been examined on control membranes from rat brain primary cell cultures and on membrane modified by culturing the cells in media supplemented with polyunsaturated fatty acids. The relationship between beta-N-acetyl-D-glucosaminidase activity and the membrane phospholipid acyl-chain composition has been evaluated. An increase in the unsaturation level of phosphatidyl ethanolamines and phosphatidylcholines, the most abundant phospholipids in this membrane fraction, is related to the rate of the enzymic reaction. The Arrhenius plot of the enzyme activity in modified membranes shows break-temperatures, starting from approximately 15 degrees C. The apparent activation energy below and above the break-temperature is not correlated with phospholipid acyl-chain unsaturation.
已在大鼠脑原代细胞培养物的对照膜以及通过在补充了多不饱和脂肪酸的培养基中培养细胞而修饰的膜上,研究了膜结合溶酶体β-N-乙酰-D-氨基葡萄糖苷酶对磷脂酰基链的依赖性。已评估了β-N-乙酰-D-氨基葡萄糖苷酶活性与膜磷脂酰基链组成之间的关系。该膜组分中最丰富的磷脂——磷脂酰乙醇胺和磷脂酰胆碱的不饱和度增加与酶促反应速率相关。修饰膜中酶活性的阿伦尼乌斯曲线显示出断裂温度,起始温度约为15℃。断裂温度上下的表观活化能与磷脂酰基链不饱和度无关。