Khokhlov A P, Baskaeva T S, Khrustaleva N A
Biull Eksp Biol Med. 1986 Oct;102(10):430-2.
A proteolytic enzyme with the activity of 8-26 U/mg protein was isolated from purified animal myelin preparation obtained by an original technique. The optimal pH of the enzyme was found to be 9.6-9.8. Its substrate specificity was studied. An enzyme with similar characteristics and identical electrophoretic mobility was isolated from the blood serum of patients with disseminated sclerosis and then purified. The major part of the enzyme activity in the blood and myelin was bound and was manifested only after special treatment. It is suggested that a similar proteolytic enzyme is present in human myelin, whose activation in demyelinating diseases may result in myelin destruction.
从采用原创技术获得的纯化动物髓磷脂制剂中分离出一种蛋白水解酶,其活性为8 - 26 U/mg蛋白质。发现该酶的最适pH值为9.6 - 9.8。对其底物特异性进行了研究。从多发性硬化症患者的血清中分离出一种具有相似特性和相同电泳迁移率的酶,然后进行了纯化。血液和髓磷脂中大部分酶活性是结合的,只有经过特殊处理才会表现出来。有人提出,人髓磷脂中存在一种类似的蛋白水解酶,其在脱髓鞘疾病中的激活可能导致髓磷脂破坏。