Rossowska M
Neurochem Res. 1979 Dec;4(6):723-9. doi: 10.1007/BF00964469.
In this study an attempt was made to elucidate the possible mechanism of the brain microsomal (Na+-K+)ATPase inhibition based on the assumption that glycoprotein part of the enzyme is exposed on the outer membrane surface. In our experiments the modification with concanavalin A of sugar end groups exposed by neuraminidase treatment resulted in a significant decrease of the brain (Na+-K+)ATPase activity. The percentage of the enzyme inhibition by concanavalin A binding to the neuraminidase-treated preparation corresponds to the amount of liberated sialic acids. The modification of the glycoprotein part of the brain (Na+-K+)ATPase complex by neuraminidase and concanavalin A treatments did not affect K+-nitrophenylphosphatase activity.
在本研究中，基于酶的糖蛋白部分暴露于外膜表面这一假设，试图阐明脑微粒体（Na⁺-K⁺）ATP酶抑制的可能机制。在我们的实验中，用伴刀豆球蛋白A对经神经氨酸酶处理后暴露的糖端基进行修饰，导致脑（Na⁺-K⁺）ATP酶活性显著降低。伴刀豆球蛋白A与经神经氨酸酶处理的制剂结合对酶的抑制百分比与释放的唾液酸量相对应。用神经氨酸酶和伴刀豆球蛋白A处理对脑（Na⁺-K⁺）ATP酶复合物糖蛋白部分的修饰并不影响K⁺-对硝基苯磷酸酶活性。
