通过使用外源性髓鞘碱性蛋白作为酶底物引发的人髓鞘酸性内肽酶活性。

Acid endopeptidase activity of human myelin, elicited by using exogenous myelin basic protein as enzyme substrate.

作者信息

Berlet H H

出版信息

FEBS Lett. 1986 Jan 6;194(2):297-300. doi: 10.1016/0014-5793(86)80104-1.

Abstract

Purified human myelin was incubated with exogenous myelin basic protein (MBP) at pH 4.0 to see if there is acid proteinase activity associated with myelin. Following incubation for 12 h up to 70% of MBP was degraded. On electrophoresis peptide fragments of MBP between 15.8 and 9.4 kDa were consistent with an endopeptic cleavage of MBP. Unlike the exogenous substrate MBP associated with myelin was only slightly degraded under the experimental conditions used. The results show that proteinase activity associated with isolated myelin may be elicited and further evaluated by using MBP as enzyme substrate.

摘要

将纯化的人髓磷脂与外源性髓磷脂碱性蛋白（MBP）在pH 4.0条件下孵育，以观察是否存在与髓磷脂相关的酸性蛋白酶活性。孵育12小时后，高达70%的MBP被降解。在电泳中，MBP的15.8至9.4 kDa的肽片段与MBP的内肽酶切割一致。与外源性底物不同，在所用实验条件下，与髓磷脂相关的MBP仅被轻微降解。结果表明，通过使用MBP作为酶底物，可以引发并进一步评估与分离的髓磷脂相关的蛋白酶活性。