Goldstein M E, Sternberger N H, Sternberger L A
J Neuroimmunol. 1987 Mar;14(2):149-60. doi: 10.1016/0165-5728(87)90049-x.
During incubation with phosphatase, the 200 kDa neurofilament protein in cytoskeletal preparations is degraded extensively. Degradation, which is divalent cation-independent, does not occur when inhibitors of phosphatase are added. The 160 kDa chymotryptic fragment of neurofilaments or affinity-purified 200 kDa protein are not degraded by phosphatase. The results suggest that phosphorylated neurofilaments are protected against proteolysis, and dephosphorylated neurofilaments are degraded by a calcium-independent, endogenous proteinase which is associated with assembled neurofilaments or with other cytoskeletal components, and not with the phosphatase used.
在与磷酸酶孵育过程中，细胞骨架制剂中的200 kDa神经丝蛋白被大量降解。这种降解不依赖二价阳离子，添加磷酸酶抑制剂时不会发生。神经丝的160 kDa胰凝乳蛋白酶片段或亲和纯化的200 kDa蛋白不会被磷酸酶降解。结果表明，磷酸化的神经丝受到蛋白水解的保护，而去磷酸化的神经丝被一种不依赖钙的内源性蛋白酶降解，该蛋白酶与组装好的神经丝或其他细胞骨架成分相关，而与所用的磷酸酶无关。
