Vandenbranden M, De Gand G, Brasseur R, Defrise-Quertain F, Ruysschaert J M
Biosci Rep. 1985 Jun;5(6):477-82. doi: 10.1007/BF01116946.
We have measured the rate of hydrolysis of liposomes made of DL-alpha-dipalmitoylphosphatidylcholine (DPPC) and L-alpha-dimyristoylphosphatidylcholine by a soluble fraction of highly purified lysosomes isolated from rat liver. Phospholipids are hydrolyzed into lysophospholipids and fatty acids at a rate which is maximal near the temperature characteristic of the gel to liquid crystalline phase transition of the lipid bilayer. This strong influence of the physical properties of the substrate on the enzyme activity suggests a structural analogy between the lysosomal phospholipases of the A type (EC 3.1.1.32 and EC 3.1.1.4) and the pancreatic phospholipase A2.
我们已测定了由二油酰磷脂酰胆碱（DPPC）和二肉豆蔻酰磷脂酰胆碱制成的脂质体的水解速率，所用的是从大鼠肝脏中分离出的高度纯化的溶酶体的可溶性部分。磷脂被水解为溶血磷脂和脂肪酸，其水解速率在接近脂质双层凝胶态到液晶态相变的特征温度时达到最大值。底物物理性质对酶活性的这种强烈影响表明，A型溶酶体磷脂酶（EC 3.1.1.32和EC 3.1.1.4）与胰腺磷脂酶A2之间存在结构相似性。
