Takamura K, Hayakawa M
Int J Biochem. 1985;17(7):831-4. doi: 10.1016/0020-711x(85)90272-1.
The effect of phospholipase A2 on the Ca2+-ATPase (EC 3.6.1.3) activity in the microsomal fraction of rat submandibular gland was kinetically studied in vitro. The Ca2+-ATPase activity was significantly increased by the treatment with phospholipase A2 in the presence of bovine serum albumin as a scavenger for hydrolyzed products. When the microsomal fraction was incubated with phospholipase A2 in the absence of bovine serum albumin, the Ca2+-ATPase activity was not altered. The Vmax and Km values for both ATP and Ca2+ were increased by the phospholipase A2 treatment, respectively. These results indicated that the activation of Ca2+-ATPase by the phospholipase A2 treatment is due to the increase of Vmax.
在体外对大鼠下颌下腺微粒体部分中磷脂酶A2对Ca2 + -ATP酶（EC 3.6.1.3）活性的影响进行了动力学研究。在存在牛血清白蛋白作为水解产物清除剂的情况下，用磷脂酶A2处理可使Ca2 + -ATP酶活性显著增加。当微粒体部分在不存在牛血清白蛋白的情况下与磷脂酶A2一起孵育时，Ca2 + -ATP酶活性没有改变。磷脂酶A2处理分别使ATP和Ca2 +的Vmax和Km值增加。这些结果表明，磷脂酶A2处理对Ca2 + -ATP酶的激活是由于Vmax的增加。
